{{Short description|Protein found in humans}} {{about|the tumor suppressor APC, in which mutations lead to colon cancer|the cell-cycle regulatory complex, APC/C|Anaphase-promoting complex}} {{Infobox gene}}
'''Adenomatous polyposis coli''' ('''APC''') also known as '''deleted in polyposis 2.5''' ('''DP2.5''') is a protein that in humans is encoded by the ''APC'' gene.<ref name="pmid1651563">{{cite journal | vauthors = Nishisho I, Nakamura Y, Miyoshi Y, Miki Y, Ando H, Horii A, Koyama K, Utsunomiya J, Baba S, Hedge P | display-authors = 6 | title = Mutations of chromosome 5q21 genes in FAP and colorectal cancer patients | journal = Science | volume = 253 | issue = 5020 | pages = 665–669 | date = August 1991 | pmid = 1651563 | doi = 10.1126/science.1651563 | bibcode = 1991Sci...253..665N }}</ref> The APC protein is a negative regulator that controls beta-catenin concentrations and interacts with E-cadherin, which are involved in cell adhesion. Mutations in the ''APC'' gene may result in colorectal cancer and desmoid tumors.<ref name="Markowitz_2009">{{cite journal | vauthors = Markowitz SD, Bertagnolli MM | title = Molecular origins of cancer: Molecular basis of colorectal cancer | journal = The New England Journal of Medicine | volume = 361 | issue = 25 | pages = 2449–2460 | date = December 2009 | pmid = 20018966 | pmc = 2843693 | doi = 10.1056/NEJMra0804588 }}</ref><ref name=":1" />
''APC'' is classified as a tumor suppressor gene. Tumor suppressor genes prevent the uncontrolled growth of cells that may result in cancerous tumors. The protein made by the ''APC'' gene plays a critical role in several cellular processes that determine whether a cell may develop into a tumor. The APC protein helps control how often a cell divides, how it attaches to other cells within a tissue, how the cell polarizes and the morphogenesis of the 3D structures,<ref>{{cite journal | vauthors = Lesko AC, Goss KH, Yang FF, Schwertner A, Hulur I, Onel K, Prosperi JR | title = The APC tumor suppressor is required for epithelial cell polarization and three-dimensional morphogenesis | journal = Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | volume = 1853 | issue = 3 | pages = 711–723 | date = March 2015 | pmid = 25578398 | pmc = 4327896 | doi = 10.1016/j.bbamcr.2014.12.036 }}</ref> or whether a cell moves within or away from tissue. This protein also helps ensure that the chromosome number in cells produced through cell division is correct. The APC protein accomplishes these tasks mainly through association with other proteins, especially those that are involved in cell attachment and signaling. The activity of one protein in particular, beta-catenin, is controlled by the APC protein (see: Wnt signaling pathway). Regulation of beta-catenin prevents genes that stimulate cell division from being turned on too often and prevents cell overgrowth.
The human ''APC'' gene is located on the long (q) arm of chromosome 5 in band q22.2 (5q22.2). The ''APC'' gene has been shown to contain an internal ribosome entry site. ''APC'' orthologs<ref name="OrthoMaM">{{cite web|title=OrthoMaM phylogenetic marker: APC coding sequence |url=http://www.orthomam.univ-montp2.fr/orthomam/data/cds/detailMarkers/ENSG00000134982_APC.xml }}{{dead link|date=December 2016 |bot=InternetArchiveBot |fix-attempted=yes }}</ref> have also been identified in all mammals for which complete genome data are available.
== Structure ==
The full-length human protein comprises 2,843 amino acids with a (predicted) molecular mass of 311646 Da. Several N-terminal domains have been structurally elucidated in unique atomistic high-resolution complex structures. Most of the protein is predicted to be intrinsically disordered. It is not known if this large predicted unstructured region from amino acid 800 to 2843 persists ''in vivo'' or would form stabilised complexes – possibly with yet unidentified interacting proteins.<ref name="pmid21859464">{{cite journal | vauthors = Minde DP, Anvarian Z, Rüdiger SG, Maurice MM | title = Messing up disorder: how do missense mutations in the tumor suppressor protein APC lead to cancer? | journal = Molecular Cancer | volume = 10 | page = 101 | date = August 2011 | pmid = 21859464 | pmc = 3170638 | doi = 10.1186/1476-4598-10-101 | doi-access = free }}</ref> Recently, it has been experimentally confirmed that the mutation cluster region around the center of APC is intrinsically disordered ''in vitro''.<ref name="APC-MCR">{{cite journal | vauthors = Minde DP, Radli M, Forneris F, Maurice MM, Rüdiger SG | title = Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutations | journal = PLOS ONE | volume = 8 | issue = 10 | article-number = e77257 | year = 2013 | pmid = 24130866 | pmc = 3793970 | doi = 10.1371/journal.pone.0077257 | doi-access = free | bibcode = 2013PLoSO...877257M }}</ref>
== Role in cancer ==
The most common mutation in colon cancer is inactivation of APC. In absence of APC inactivating mutations, colon cancers commonly carry activating mutations in beta catenin or inactivating mutations in RNF43.<ref name=":0" /> Mutations in APC can be inherited, or arise sporadically in the somatic cells, often as the result of mutations in other genes that result in the inability to repair mutations in the DNA. In order for cancer to develop, both alleles (copies of the APC gene) must be mutated. Mutations in APC or β-catenin must be followed by other mutations to become cancerous; however, in carriers of an APC-inactivating mutation, the risk of colorectal cancer by age 40 is almost 100%.<ref name="Markowitz_2009"/>
Familial adenomatous polyposis (FAP) is caused by an inherited, inactivating mutation in the APC gene.<ref>{{cite web |url=https://www.lecturio.com/concepts/familial-adenomatous-polyposis/ | title=Familial Adenomatous Polyposis | website=The Lecturio Medical Concept Library |access-date= 22 July 2021}}</ref> More than 800 mutations {{Citation needed|date=November 2008}} in the ''APC'' gene have been identified in families with classic and attenuated types of familial adenomatous polyposis. Most of these mutations cause the production of an APC protein that is abnormally short and presumably nonfunctional. This short protein cannot suppress the cellular overgrowth that leads to the formation of polyps, which can become cancerous. The most common mutation in familial adenomatous polyposis is a deletion of five bases in the ''APC'' gene. This mutation changes the sequence of amino acids in the resulting APC protein beginning at position 1309. Mutations in the ''APC'' gene have also been found to lead to the development of desmoid tumors in FAP patients.<ref name=":1">{{cite journal | vauthors = Howard JH, Pollock RE | title = Intra-Abdominal and Abdominal Wall Desmoid Fibromatosis | journal = Oncology and Therapy | volume = 4 | issue = 1 | pages = 57–72 | date = June 2016 | pmid = 28261640 | pmc = 5315078 | doi = 10.1007/s40487-016-0017-z }}</ref>
Another mutation is carried by approximately 6 percent{{citation needed|date=April 2023}} of people of Ashkenazi (eastern and central European) Jewish heritage. This mutation results in the substitution of the amino acid lysine for isoleucine at position 1307 in the APC protein (also written as I1307K or Ile1307Lys). This change has been shown to be associated with an increased risk of colon cancer,<ref>{{cite journal | vauthors = Liang J, Lin C, Hu F, Wang F, Zhu L, Yao X, Wang Y, Zhao Y | display-authors = 6 | title = APC polymorphisms and the risk of colorectal neoplasia: a HuGE review and meta-analysis | journal = American Journal of Epidemiology | volume = 177 | issue = 11 | pages = 1169–1179 | date = June 2013 | pmid = 23576677 | doi = 10.1093/aje/kws382 | doi-access = free }}</ref> with moderate effect size.<ref name=Forkosh2022>{{cite journal | vauthors = Forkosh E, Bergel M, Hatchell KE, Nielsen SM, Heald B, Benson AA, Friedman E, Esplin ED, Katz LH | display-authors = 6 | title = Ashkenazi Jewish and Other White ''APC'' I1307K Carriers Are at Higher Risk for Multiple Cancers | journal = Cancers | volume = 14 | issue = 23 | page = 5875 | date = November 2022 | pmid = 36497357 | pmc = 9740723 | doi = 10.3390/cancers14235875 | id = 5875 | doi-access = free }}</ref> APC I1307K has also been implicated as a risk factor for certain other cancers.<ref name=Forkosh2022/>
== Regulation of proliferation ==
The (Adenomatous Polyposis Coli) APC protein normally builds a "destruction complex" with glycogen synthase kinase 3-alpha and or beta (GSK-3α/β) and Axin via interactions with the 20 AA and SAMP repeats.<ref>{{cite journal | vauthors = Rubinfeld B, Albert I, Porfiri E, Fiol C, Munemitsu S, Polakis P | title = Binding of GSK3beta to the APC-beta-catenin complex and regulation of complex assembly | journal = Science | volume = 272 | issue = 5264 | pages = 1023–1026 | date = May 1996 | pmid = 8638126 | doi = 10.1126/science.272.5264.1023 | s2cid = 84899068 | bibcode = 1996Sci...272.1023R }}</ref><ref>{{cite journal | vauthors = Kishida S, Yamamoto H, Ikeda S, Kishida M, Sakamoto I, Koyama S, Kikuchi A | title = Axin, a negative regulator of the wnt signaling pathway, directly interacts with adenomatous polyposis coli and regulates the stabilization of beta-catenin | journal = The Journal of Biological Chemistry | volume = 273 | issue = 18 | pages = 10823–10826 | date = May 1998 | pmid = 9556553 | doi = 10.1074/jbc.273.18.10823 | doi-access = free }}</ref><ref name="pmid9734785"/> This complex is then able to bind β-catenins in the cytoplasm, that have dissociated from adherens contacts between cells. With the help of casein kinase 1 (CK1), which carries out an initial phosphorylation of β-catenin, GSK-3β is able to phosphorylate β-catenin a second time. This targets β-catenin for ubiquitination and degradation by cellular proteasomes. This prevents it from translocating into the nucleus, where it acts as a transcription factor for proliferation genes.<ref name="pmid19287945">{{cite journal | vauthors = Leber MF, Efferth T | title = Molecular principles of cancer invasion and metastasis (review) | journal = International Journal of Oncology | volume = 34 | issue = 4 | pages = 881–895 | date = April 2009 | pmid = 19287945 | doi = 10.3892/ijo_00000214 | doi-access = free }}</ref> ''APC'' is also thought to be targeted to microtubules via the PDZ binding domain, stabilizing them.<ref>{{cite journal | vauthors = Wen Y, Eng CH, Schmoranzer J, Cabrera-Poch N, Morris EJ, Chen M, Wallar BJ, Alberts AS, Gundersen GG | display-authors = 6 | title = EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration | journal = Nature Cell Biology | volume = 6 | issue = 9 | pages = 820–830 | date = September 2004 | pmid = 15311282 | doi = 10.1038/ncb1160 | s2cid = 29214110 }}</ref> The deactivation of the APC protein can take place after certain chain reactions in the cytoplasm are started, e.g. through the Wnt signals that destroy the conformation of the complex.{{Citation needed|date=May 2012}} In the nucleus it complexes with legless/BCL9, TCF, and Pygo.{{Citation needed|date=May 2012}}
The ability of ''APC'' to bind β-catenin has been classically considered to be an integral part of the protein's mechanistic function in the destruction complex, along with binding to Axin through the SAMP repeats.<ref>{{cite journal | vauthors = Stamos JL, Weis WI | title = The β-catenin destruction complex | journal = Cold Spring Harbor Perspectives in Biology | volume = 5 | issue = 1 | article-number = a007898 | date = January 2013 | pmid = 23169527 | pmc = 3579403 | doi = 10.1101/cshperspect.a007898 }}</ref> These models have been substantiated by observations that common APC loss of function mutations in the mutation cluster region often remove several β-catenin binding sites and SAMP repeats. However, recent evidence from Yamulla and colleagues have directly tested those models and imply that APC's core mechanistic functions may not require direct binding to β-catenin, but necessitate interactions with Axin.<ref>{{cite journal | vauthors = Yamulla RJ, Kane EG, Moody AE, Politi KA, Lock NE, Foley AV, Roberts DM | title = Testing models of the APC tumor suppressor/β-catenin interaction reshapes our view of the destruction complex in Wnt signaling | journal = Genetics | volume = 197 | issue = 4 | pages = 1285–1302 | date = August 2014 | pmid = 24931405 | pmc = 4125400 | doi = 10.1534/genetics.114.166496 }}</ref> The researchers hypothesized that APC's many β-catenin binding sites increase the protein's efficiency at destroying β-catenin, yet are not absolutely necessary for the protein's mechanistic function. Further research is clearly necessary to elucidate the precise mechanistic function of APC in the destruction complex.{{cn|date=March 2025}}
== Mutations == [[File:Familial Adenomatous Polyposis intestine.jpg|thumb|Familial adenomatous polyposis of the intestine]] Mutations in ''APC'' often occur early on in cancers such as colon cancer.<ref name="pmid21859464"/> Patients with familial adenomatous polyposis (FAP) have germline mutations, with 95% being nonsense/frameshift mutations leading to premature stop codons. 33% of mutations occur between amino acids 1061–1309. In somatic mutations, over 60% occur within a mutation cluster region (1286–1513), causing loss of axin-binding sites in all but one of the 20AA repeats. Mutations in ''APC'' lead to loss of β-catenin regulation, altered cell migration and chromosome instability.<ref name=":0">{{cite journal | vauthors = Bugter JM, Fenderico N, Maurice MM | title = Mutations and mechanisms of WNT pathway tumour suppressors in cancer | journal = Nature Reviews. Cancer | volume = 21 | issue = 1 | pages = 5–21 | date = January 2021 | pmid = 33097916 | doi = 10.1038/s41568-020-00307-z | s2cid = 225058221 }}</ref>
== Neurological role ==
Rosenberg ''et al.'' found that ''APC'' directs cholinergic synapse assembly between neurons, a finding with implications for autonomic neuropathies, for Alzheimer's disease, for age-related hearing loss, and for some forms of epilepsy and schizophrenia.<ref>{{cite journal | vauthors = Rosenberg MM, Yang F, Mohn JL, Storer EK, Jacob MH | title = The postsynaptic adenomatous polyposis coli (APC) multiprotein complex is required for localizing neuroligin and neurexin to neuronal nicotinic synapses in vivo | journal = The Journal of Neuroscience | volume = 30 | issue = 33 | pages = 11073–11085 | date = August 2010 | pmid = 20720115 | pmc = 2945243 | doi = 10.1523/JNEUROSCI.0983-10.2010 }}</ref> <sup>(29)</sup>
== Interactions ==
''APC'' (gene) has been shown to interact with: {{div col|colwidth=20em}} * ARHGEF4,<ref name = pmid10947987>{{cite journal | vauthors = Kawasaki Y, Senda T, Ishidate T, Koyama R, Morishita T, Iwayama Y, Higuchi O, Akiyama T | display-authors = 6 | title = Asef, a link between the tumor suppressor APC and G-protein signaling | journal = Science | volume = 289 | issue = 5482 | pages = 1194–1197 | date = August 2000 | pmid = 10947987 | doi = 10.1126/science.289.5482.1194 | bibcode = 2000Sci...289.1194K }}</ref> * AXIN1,<ref name = pmid9734785>{{cite journal | vauthors = Nakamura T, Hamada F, Ishidate T, Anai K, Kawahara K, Toyoshima K, Akiyama T | title = Axin, an inhibitor of the Wnt signalling pathway, interacts with beta-catenin, GSK-3beta and APC and reduces the beta-catenin level | journal = Genes to Cells | volume = 3 | issue = 6 | pages = 395–403 | date = June 1998 | pmid = 9734785 | doi = 10.1046/j.1365-2443.1998.00198.x | doi-access = free }}</ref> * BUB1,<ref name = pmid11283619>{{cite journal | vauthors = Kaplan KB, Burds AA, Swedlow JR, Bekir SS, Sorger PK, Näthke IS | title = A role for the Adenomatous Polyposis Coli protein in chromosome segregation | journal = Nature Cell Biology | volume = 3 | issue = 4 | pages = 429–432 | date = April 2001 | pmid = 11283619 | doi = 10.1038/35070123 | s2cid = 12645435 }}</ref> * CTNNB1,<ref name = pmid8259519>{{cite journal | vauthors = Su LK, Vogelstein B, Kinzler KW | title = Association of the APC tumor suppressor protein with catenins | journal = Science | volume = 262 | issue = 5140 | pages = 1734–1737 | date = December 1993 | pmid = 8259519 | doi = 10.1126/science.8259519 | bibcode = 1993Sci...262.1734S }}</ref><ref name = pmid11712088>{{cite journal | vauthors = Kucerová D, Sloncová E, Tuhácková Z, Vojtechová M, Sovová V | title = Expression and interaction of different catenins in colorectal carcinoma cells | journal = International Journal of Molecular Medicine | volume = 8 | issue = 6 | pages = 695–698 | date = December 2001 | pmid = 11712088 | doi = 10.3892/ijmm.8.6.695 }}</ref><ref name = pmid12628243>{{cite journal | vauthors = Tickenbrock L, Kössmeier K, Rehmann H, Herrmann C, Müller O | title = Differences between the interaction of beta-catenin with non-phosphorylated and single-mimicked phosphorylated 20-amino acid residue repeats of the APC protein | journal = Journal of Molecular Biology | volume = 327 | issue = 2 | pages = 359–367 | date = March 2003 | pmid = 12628243 | doi = 10.1016/S0022-2836(03)00144-X }}</ref><ref name = pmid11251183>{{cite journal | vauthors = Davies G, Jiang WG, Mason MD | title = The interaction between beta-catenin, GSK3beta and APC after motogen induced cell-cell dissociation, and their involvement in signal transduction pathways in prostate cancer | journal = International Journal of Oncology | volume = 18 | issue = 4 | pages = 843–847 | date = April 2001 | pmid = 11251183 | doi = 10.3892/ijo.18.4.843 }}</ref><ref name = pmid11533658>{{cite journal | vauthors = Ryo A, Nakamura M, Wulf G, Liou YC, Lu KP | title = Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC | journal = Nature Cell Biology | volume = 3 | issue = 9 | pages = 793–801 | date = September 2001 | pmid = 11533658 | doi = 10.1038/ncb0901-793 | s2cid = 664553 }}</ref><ref name = pmid11972058/><ref name = pmid9286858>{{cite journal | vauthors = Satoh K, Yanai H, Senda T, Kohu K, Nakamura T, Okumura N, Matsumine A, Kobayashi S, Toyoshima K, Akiyama T | display-authors = 6 | title = DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95 | journal = Genes to Cells | volume = 2 | issue = 6 | pages = 415–424 | date = June 1997 | pmid = 9286858 | doi = 10.1046/j.1365-2443.1997.1310329.x | doi-access = free }}</ref><ref name = pmid11707392>{{cite journal | vauthors = Eklof Spink K, Fridman SG, Weis WI | title = Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex | journal = The EMBO Journal | volume = 20 | issue = 22 | pages = 6203–6212 | date = November 2001 | pmid = 11707392 | pmc = 125720 | doi = 10.1093/emboj/20.22.6203 }}</ref> * CSNK2B,<ref name = pmid11972058>{{cite journal | vauthors = Homma MK, Li D, Krebs EG, Yuasa Y, Homma Y | title = Association and regulation of casein kinase 2 activity by adenomatous polyposis coli protein | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 9 | pages = 5959–5964 | date = April 2002 | pmid = 11972058 | pmc = 122884 | doi = 10.1073/pnas.092143199 | doi-access = free | bibcode = 2002PNAS...99.5959K }}</ref> * CSNK2A1,<ref name = pmid11972058/> * Catenin (cadherin-associated protein), alpha 1,<ref name = pmid8259519/><ref name = pmid7651399/> * DLG3,<ref name = pmid9188857>{{cite journal | vauthors = Makino K, Kuwahara H, Masuko N, Nishiyama Y, Morisaki T, Sasaki J, Nakao M, Kuwano A, Nakata M, Ushio Y, Saya H | display-authors = 6 | title = Cloning and characterization of NE-dlg: a novel human homolog of the Drosophila discs large (dlg) tumor suppressor protein interacts with the APC protein | journal = Oncogene | volume = 14 | issue = 20 | pages = 2425–2433 | date = May 1997 | pmid = 9188857 | doi = 10.1038/sj.onc.1201087 | doi-access = free }}</ref> * KIFAP3,<ref name = pmid11912492>{{cite journal | vauthors = Jimbo T, Kawasaki Y, Koyama R, Sato R, Takada S, Haraguchi K, Akiyama T | title = Identification of a link between the tumour suppressor APC and the kinesin superfamily | journal = Nature Cell Biology | volume = 4 | issue = 4 | pages = 323–327 | date = April 2002 | pmid = 11912492 | doi = 10.1038/ncb779 | s2cid = 10745049 }}</ref> * MAPRE2,<ref name = pmid7606712>{{cite journal | vauthors = Su LK, Burrell M, Hill DE, Gyuris J, Brent R, Wiltshire R, Trent J, Vogelstein B, Kinzler KW | display-authors = 6 | title = APC binds to the novel protein EB1 | journal = Cancer Research | volume = 55 | issue = 14 | pages = 2972–2977 | date = July 1995 | pmid = 7606712 }}</ref><ref name = pmid11470413>{{cite journal | vauthors = Nakamura M, Zhou XZ, Lu KP | title = Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization | journal = Current Biology | volume = 11 | issue = 13 | pages = 1062–1067 | date = July 2001 | pmid = 11470413 | doi = 10.1016/S0960-9822(01)00297-4 | s2cid = 14122895 | doi-access = free | bibcode = 2001CBio...11.1062N }}</ref> * JUP,<ref name = pmid7651399>{{cite journal | vauthors = Daniel JM, Reynolds AB | title = The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin | journal = Molecular and Cellular Biology | volume = 15 | issue = 9 | pages = 4819–4824 | date = September 1995 | pmid = 7651399 | pmc = 230726 | doi = 10.1128/mcb.15.9.4819 }}</ref><ref name = pmid8074697>{{cite journal | vauthors = Shibata T, Gotoh M, Ochiai A, Hirohashi S | title = Association of plakoglobin with APC, a tumor suppressor gene product, and its regulation by tyrosine phosphorylation | journal = Biochemical and Biophysical Research Communications | volume = 203 | issue = 1 | pages = 519–522 | date = August 1994 | pmid = 8074697 | doi = 10.1006/bbrc.1994.2213 }}</ref> * SIAH1,<ref name = pmid11389840>{{cite journal | vauthors = Liu J, Stevens J, Rote CA, Yost HJ, Hu Y, Neufeld KL, White RL, Matsunami N | display-authors = 6 | title = Siah-1 mediates a novel beta-catenin degradation pathway linking p53 to the adenomatous polyposis coli protein | journal = Molecular Cell | volume = 7 | issue = 5 | pages = 927–936 | date = May 2001 | pmid = 11389840 | doi = 10.1016/S1097-2765(01)00241-6 | doi-access = free }}</ref> * TFAP2A,<ref name = pmid15331612>{{cite journal | vauthors = Li Q, Dashwood RH | title = Activator protein 2alpha associates with adenomatous polyposis coli/beta-catenin and Inhibits beta-catenin/T-cell factor transcriptional activity in colorectal cancer cells | journal = The Journal of Biological Chemistry | volume = 279 | issue = 44 | pages = 45669–45675 | date = October 2004 | pmid = 15331612 | pmc = 2276578 | doi = 10.1074/jbc.M405025200 | doi-access = free }}</ref> * TUBA4A<ref name = pmid11166179>{{cite journal | vauthors = Zumbrunn J, Kinoshita K, Hyman AA, Näthke IS | title = Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3 beta phosphorylation | journal = Current Biology | volume = 11 | issue = 1 | pages = 44–49 | date = January 2001 | pmid = 11166179 | doi = 10.1016/S0960-9822(01)00002-1 | s2cid = 15004529 | doi-access = free | bibcode = 2001CBio...11...44Z }}</ref> and * XPO1.<ref name = pmid12070164>{{cite journal | vauthors = Tickenbrock L, Cramer J, Vetter IR, Muller O | title = The coiled coil region (amino acids 129-250) of the tumor suppressor protein adenomatous polyposis coli (APC). Its structure and its interaction with chromosome maintenance region 1 (Crm-1) | journal = The Journal of Biological Chemistry | volume = 277 | issue = 35 | pages = 32332–32338 | date = August 2002 | pmid = 12070164 | doi = 10.1074/jbc.M203990200 | doi-access = free }}</ref> {{Div col end}}
[[Image:Signal transduction pathways.svg|300px|thumb|center|Overview of signal transduction pathways involved in apoptosis.]]
== See also == * MUTYH
== References == {{reflist|33em}}
== Further reading == {{refbegin|33em}} * {{cite journal | vauthors = Cohen MM | title = Molecular dimensions of gastrointestinal tumors: some thoughts for digestion | journal = American Journal of Medical Genetics. Part A | volume = 122A | issue = 4 | pages = 303–314 | date = November 2003 | pmid = 14518068 | doi = 10.1002/ajmg.a.20473 | s2cid = 9546199 }} * {{cite journal | vauthors = Fearnhead NS, Britton MP, Bodmer WF | title = The ABC of APC | journal = Human Molecular Genetics | volume = 10 | issue = 7 | pages = 721–733 | date = April 2001 | pmid = 11257105 | doi = 10.1093/hmg/10.7.721 | doi-access = free }} * {{cite journal | vauthors = Fodde R | title = The APC gene in colorectal cancer | journal = European Journal of Cancer | volume = 38 | issue = 7 | pages = 867–871 | date = May 2002 | pmid = 11978510 | doi = 10.1016/S0959-8049(02)00040-0 }} * {{cite journal | vauthors = Goss KH, Groden J | title = Biology of the adenomatous polyposis coli tumor suppressor | journal = Journal of Clinical Oncology | volume = 18 | issue = 9 | pages = 1967–1979 | date = May 2000 | pmid = 10784639 | doi = 10.1200/JCO.2000.18.9.1967 }} * {{cite journal | vauthors = Järvinen HJ, Peltomäki P | title = The complex genotype-phenotype relationship in familial adenomatous polyposis | journal = European Journal of Gastroenterology & Hepatology | volume = 16 | issue = 1 | pages = 5–8 | date = January 2004 | pmid = 15095846 | doi = 10.1097/00042737-200401000-00002 | s2cid = 20780391 }} * {{cite journal | vauthors = Lal G, Gallinger S | title = Familial adenomatous polyposis | journal = Seminars in Surgical Oncology | volume = 18 | issue = 4 | pages = 314–323 | date = June 2000 | pmid = 10805953 | doi = 10.1002/(SICI)1098-2388(200006)18:4<314::AID-SSU6>3.0.CO;2-9 }} * {{cite journal | vauthors = van Es JH, Giles RH, Clevers HC | title = The many faces of the tumor suppressor gene APC | journal = Experimental Cell Research | volume = 264 | issue = 1 | pages = 126–134 | date = March 2001 | pmid = 11237529 | doi = 10.1006/excr.2000.5142 }} * {{cite journal | vauthors = Rosenberg MM, Yang F, Giovanni M, Mohn JL, Temburni MK, Jacob MH | title = Adenomatous polyposis coli plays a key role, in vivo, in coordinating assembly of the neuronal nicotinic postsynaptic complex | journal = Molecular and Cellular Neurosciences | volume = 38 | issue = 2 | pages = 138–152 | date = June 2008 | pmid = 18407517 | pmc = 2502068 | doi = 10.1016/j.mcn.2008.02.006 }} {{refend}}
== External links == * [https://www.ncbi.nlm.nih.gov/books/NBK1345/ GeneReviews/NCBI/NIH/UW entry on APC-Associated Polyposis Conditions] * [https://archive.today/20121213231156/http://www.ncbi.nlm.nih.gov/omim/175100,276300,611731,175100,276300,611731 OMIM entries on APC-Associated Polyposis Conditions] * {{MeshName|Adenomatous+Polyposis+Coli+Protein}} * [https://web.archive.org/web/20160121162032/http://www.genecards.org/cgi-bin/carddisp?APC GeneCard] * [http://webarchive.loc.gov/all/20090609091852/http://tools.niehs.nih.gov/gac/datamining/index.cfm Database concerning peer-reviewed reports on cancer critical alteration in several genes including (APC (protein)), (TP53), (Beta-catenin|β-catenin)] * {{UCSC gene info|APC}}
{{PDB Gallery|geneid=324}} {{Tumor suppressor genes}} {{Cytoskeletal Proteins}} {{Wnt signaling pathway}}
{{DEFAULTSORT:Apc (Protein)}} Category:Human proteins Category:Tumor suppressor genes Category:Armadillo-repeat-containing proteins