{{Short description|Protein-coding gene in the species Homo sapiens}} {{cs1 config|name-list-style=vanc}} {{Infobox_gene}} '''Lymphocyte cytosolic protein 2''' (SH2 domain containing leukocyte protein of 76kDa), also known as '''LCP2''' or '''SLP-76''', is a signal-transducing adaptor protein expressed in T cells and myeloid cells and is important in the signaling of T-cell receptors (TCRs).<ref name="entrez">{{Cite web| title = Entrez Gene: LCP2 lymphocyte cytosolic protein 2 (SH2 domain containing leukocyte protein of 76kDa)| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=3937}}</ref><ref name="role of SLP-76">{{cite journal | vauthors = Pivniouk VI, Geha RS | title = The role of SLP-76 and LAT in lymphocyte development | journal = Current Opinion in Immunology | volume = 12 | issue = 2 | pages = 173–178 | date = April 2000 | pmid = 10712938 | doi = 10.1016/S0952-7915(99)00068-0 }}</ref> As an adaptor protein, SLP-76 does not have catalytic functions, primarily binding other signaling proteins to form larger signaling complexes.<ref name="yablonski2001" /> It is a key component of the signaling pathways of receptors with immunoreceptor tyrosine-based activation motifs (ITAMs) such as T-cell receptors, its precursors, and receptors for the Fc regions of certain antibodies.<ref name="yablonski2001">{{cite book | vauthors = Yablonski D, Weiss A | title = Mechanisms of signaling by the hematopoietic-specific adaptor proteins, SLP-76 and lat and their b cell counterpart, BLNK/SLP-65 | series = Advances in Immunology | volume = 79 | pages = 93–128 | date = 2001 | pmid = 11680012 | doi = 10.1016/S0065-2776(01)79003-7 | isbn = 978-0-12-022479-1 }}</ref> SLP-76 is expressed in T-cells and related lymphocytes like natural killer cells.<ref name="kim_NK_2012">{{cite journal | vauthors = Kim HS, Long EO | title = Complementary phosphorylation sites in the adaptor protein SLP-76 promote synergistic activation of natural killer cells | journal = Science Signaling | volume = 5 | issue = 232 | pages = ra49 | date = July 2012 | pmid = 22786724 | pmc = 3842037 | doi = 10.1126/scisignal.2002754 }}</ref>
== Structure and function == The amino acid sequence of the protein has a central domain with a high concentration of prolines, as well as domains at the amino-terminal and carboxy-terminal of the amino acid sequence. The PDB file 1H3H depicts the SH3 domain of GRAP2 in complex with an RSTK-containing peptide representing residues 226–235 of SLP-76.<ref>Structural Basis for Specific Binding of the Gads SH3 Domain to an RxxK Motif-Containing SLP-76 Peptide https://doi.org/10.1016/S1097-2765(03)00046-7</ref> The human and murine cDNAs both encode 533 amino acid proteins that are 72% identical and composed of three modular domains.<ref name="entrez"></ref> The central domain binds SRC-Homology 3 (SH3) domains of other adaptor molecules such as Grb2 and Gads. The N-terminus has an acidic region with sections for SH2-domain binding and tyrosine residues that bind the proteins Vav and Nck when phosphorylated. The C-terminus region is itself a SH2 domain and binds FYB among other proteins.<ref name="role of SLP-76"></ref> SLP-76 is triggered when the TCR binds its ligand by the phosphorylation of tyrosines on the N-terminus by ZAP-70, a tyrosine kinase. Along with the LAT (linker for activation of T cells) adaptor protein, SLP-76 is essential to nearly all downstream effects from T-cell receptor signals. SLP-76, LAT, and Gads together combine into protein complexes, typically with LAT at the center and SLP-76 proteins on the outside. These complexes associate into larger microclusters that activate a multitude of signaling pathways.<ref name="yablonski2019">{{cite journal | vauthors = Yablonski D | title = Bridging the Gap: Modulatory Roles of the Grb2-Family Adaptor, Gads, in Cellular and Allergic Immune Responses | journal = Frontiers in Immunology | volume = 10 | page = 1704 | date = July 2019 | pmid = 31402911 | doi = 10.3389/fimmu.2019.01704 | pmc = 6669380 | doi-access = free }}</ref><ref name="microclusters">{{cite journal | vauthors = Balagopalan L, Raychaudhuri K, Samelson LE | title = Microclusters as T Cell Signaling Hubs: Structure, Kinetics, and Regulation | journal = Frontiers in Cell and Developmental Biology | volume = 8 | article-number = 608530 | date = January 2021 | pmid = 33575254 | doi = 10.3389/fcell.2020.608530 | pmc = 7870797 | doi-access = free }}</ref> The proteins that bind SLP-76 are essential to the production and secretion of interleukin 2 (IL-2) and rearrangement of the actin cytoskeleton in T-cells, which is an important part of T-cell division and proliferation.<ref name="role of SLP-76"></ref>
Studies using SLP-76-deficient T cell lines or mice have provided strong evidence that SLP-76 plays a positive role more generally in promoting T cell development and activation, as well as mast cell and platelet function. SLP-76 is critical in the signaling from the pre-TCR that shifts T-cell developing thymocytes from the double-negative (DN) stage to the double-positive (DP) stage. Allelic exclusion of the second locus of the TCRβ chain is also dependent on signaling from the TCRβ chain that is first expressed, involving SLP-76 as a key intermediate.<ref name="role of SLP-76"></ref>
SLP-76 is also important in natural killer (NK) cells, in the signaling pathways of the NK cell receptors (NKRs). The SH2 domain on the C-terminus binds HPK-1, a serine-threonine kinase, and the adhesion and degranulation-promoting adaptor protein (ADAP) also known as FYB. Both these proteins are common to regular T-cells as well, but have unique downstream signaling effects in NK cells relating to their distribution across different tissues. Studies using mutations in the SH2 domain of mice show that it produces an accumulation of invariant NK cells in primary lymphoid organs like the thymus and in peripheral lymph nodes, with a simultaneous reduction of these cells in the livers and spleens.<ref name="gerth_nk cells">{{cite journal | vauthors = Gerth E, Mattner J | title = The Role of Adaptor Proteins in the Biology of Natural Killer T (NKT) Cells | journal = Frontiers in Immunology | volume = 10 | page = 1449 | date = June 2019 | pmid = 31293596 | doi = 10.3389/fimmu.2019.01449 | pmc = 6603179 | doi-access = free }}</ref>
== Interactions == Lymphocyte cytosolic protein 2 has been shown to interact with: {{div col|colwidth=20em}} * Cbl gene,<ref name="pmid10477741">{{cite journal | vauthors = Park RK, Izadi KD, Deo YM, Durden DL | title = Role of Src in the modulation of multiple adaptor proteins in FcalphaRI oxidant signaling | journal = Blood | volume = 94 | issue = 6 | pages = 2112–2120 | date = September 1999 | pmid = 10477741 | doi = 10.1182/blood.V94.6.2112 }}</ref><ref name="pmid10204582">{{cite journal | vauthors = Erdreich-Epstein A, Liu M, Kant AM, Izadi KD, Nolta JA, Durden DL | title = Cbl functions downstream of Src kinases in Fc gamma RI signaling in primary human macrophages | journal = Journal of Leukocyte Biology | volume = 65 | issue = 4 | pages = 523–534 | date = April 1999 | pmid = 10204582 | doi = 10.1002/jlb.65.4.523 | s2cid = 18340540 }}</ref> * GRAP2,<ref name="pmid16189514">{{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | display-authors = 6 | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–1178 | date = October 2005 | pmid = 16189514 | doi = 10.1038/nature04209 | s2cid = 4427026 | bibcode = 2005Natur.437.1173R }}</ref><ref name="pmid10820259">{{cite journal | vauthors = Ellis JH, Ashman C, Burden MN, Kilpatrick KE, Morse MA, Hamblin PA | title = GRID: a novel Grb-2-related adapter protein that interacts with the activated T cell costimulatory receptor CD28 | journal = Journal of Immunology | volume = 164 | issue = 11 | pages = 5805–5814 | date = June 2000 | pmid = 10820259 | doi = 10.4049/jimmunol.164.11.5805 | doi-access = free }}</ref><ref name="pmid10021361">{{cite journal | vauthors = Liu SK, Fang N, Koretzky GA, McGlade CJ | title = The hematopoietic-specific adaptor protein gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors | journal = Current Biology | volume = 9 | issue = 2 | pages = 67–75 | date = January 1999 | pmid = 10021361 | doi = 10.1016/S0960-9822(99)80017-7 | s2cid = 14131281 | doi-access = free | bibcode = 1999CBio....9...67L }}</ref><ref name="pmid10224278">{{cite journal | vauthors = Asada H, Ishii N, Sasaki Y, Endo K, Kasai H, Tanaka N, Takeshita T, Tsuchiya S, Konno T, Sugamura K | display-authors = 6 | title = Grf40, A novel Grb2 family member, is involved in T cell signaling through interaction with SLP-76 and LAT | journal = The Journal of Experimental Medicine | volume = 189 | issue = 9 | pages = 1383–1390 | date = May 1999 | pmid = 10224278 | pmc = 2193052 | doi = 10.1084/jem.189.9.1383 }}</ref> * Grb2,<ref name="pmid10204582" /><ref name="pmid10224278" /><ref name="pmid11314042">{{cite journal | vauthors = Lewitzky M, Kardinal C, Gehring NH, Schmidt EK, Konkol B, Eulitz M, Birchmeier W, Schaeper U, Feller SM | display-authors = 6 | title = The C-terminal SH3 domain of the adapter protein Grb2 binds with high affinity to sequences in Gab1 and SLP-76 which lack the SH3-typical P-x-x-P core motif | journal = Oncogene | volume = 20 | issue = 9 | pages = 1052–1062 | date = March 2001 | pmid = 11314042 | doi = 10.1038/sj.onc.1204202 | doi-access = free }}</ref><ref name="pmid8695800">{{cite journal | vauthors = Robinson A, Gibbins J, Rodríguez-Liñares B, Finan PM, Wilson L, Kellie S, Findell P, Watson SP | display-authors = 6 | title = Characterization of Grb2-binding proteins in human platelets activated by Fc gamma RIIA cross-linking | journal = Blood | volume = 88 | issue = 2 | pages = 522–530 | date = July 1996 | pmid = 8695800 | doi = 10.1182/blood.V88.2.522.bloodjournal882522 | doi-access = free }}</ref><ref name="pmid8995445">{{cite journal | vauthors = Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA | title = SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells | journal = The Journal of Biological Chemistry | volume = 272 | issue = 2 | pages = 1363–1367 | date = January 1997 | pmid = 8995445 | doi = 10.1074/jbc.272.2.1363 | doi-access = free }}</ref> * ITK<ref name="pmid15388330" /><ref name="pmid10636929">{{cite journal | vauthors = Bunnell SC, Diehn M, Yaffe MB, Findell PR, Cantley LC, Berg LJ | title = Biochemical interactions integrating Itk with the T cell receptor-initiated signaling cascade | journal = The Journal of Biological Chemistry | volume = 275 | issue = 3 | pages = 2219–2230 | date = January 2000 | pmid = 10636929 | doi = 10.1074/jbc.275.3.2219 | doi-access = free }}</ref> * LYN,<ref name="pmid10026222">{{cite journal | vauthors = Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP | display-authors = 6 | title = Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets | journal = The Journal of Biological Chemistry | volume = 274 | issue = 9 | pages = 5963–5971 | date = February 1999 | pmid = 10026222 | doi = 10.1074/jbc.274.9.5963 | doi-access = free }}</ref> * NCK1,<ref name="pmid15388330">{{cite journal | vauthors = Shim EK, Moon CS, Lee GY, Ha YJ, Chae SK, Lee JR | title = Association of the Src homology 2 domain-containing leukocyte phosphoprotein of 76 kD (SLP-76) with the p85 subunit of phosphoinositide 3-kinase | journal = FEBS Letters | volume = 575 | issue = 1–3 | pages = 35–40 | date = September 2004 | pmid = 15388330 | doi = 10.1016/j.febslet.2004.07.090 | s2cid = 24678709 | doi-access = | bibcode = 2004FEBSL.575...35S }}</ref><ref name="pmid10229072">{{cite journal | vauthors = Wunderlich L, Faragó A, Downward J, Buday L | title = Association of Nck with tyrosine-phosphorylated SLP-76 in activated T lymphocytes | journal = European Journal of Immunology | volume = 29 | issue = 4 | pages = 1068–1075 | date = April 1999 | pmid = 10229072 | doi = 10.1002/(SICI)1521-4141(199904)29:04<1068::AID-IMMU1068>3.0.CO;2-P | doi-access = free }}</ref> * PIK3R1,<ref name="pmid15388330" /> * PLCG1,<ref name="pmid11390650">{{cite journal | vauthors = Yablonski D, Kadlecek T, Weiss A | title = Identification of a phospholipase C-gamma1 (PLC-gamma1) SH3 domain-binding site in SLP-76 required for T-cell receptor-mediated activation of PLC-gamma1 and NFAT | journal = Molecular and Cellular Biology | volume = 21 | issue = 13 | pages = 4208–4218 | date = July 2001 | pmid = 11390650 | pmc = 87082 | doi = 10.1128/MCB.21.13.4208-4218.2001 }}</ref> * PTPN6,<ref name="pmid9765283">{{cite journal | vauthors = Binstadt BA, Billadeau DD, Jevremović D, Williams BL, Fang N, Yi T, Koretzky GA, Abraham RT, Leibson PJ | display-authors = 6 | title = SLP-76 is a direct substrate of SHP-1 recruited to killer cell inhibitory receptors | journal = The Journal of Biological Chemistry | volume = 273 | issue = 42 | pages = 27518–27523 | date = October 1998 | pmid = 9765283 | doi = 10.1074/jbc.273.42.27518 | doi-access = free }}</ref><ref name="pmid8760799">{{cite journal | vauthors = Mizuno K, Katagiri T, Hasegawa K, Ogimoto M, Yakura H | title = Hematopoietic cell phosphatase, SHP-1, is constitutively associated with the SH2 domain-containing leukocyte protein, SLP-76, in B cells | journal = The Journal of Experimental Medicine | volume = 184 | issue = 2 | pages = 457–463 | date = August 1996 | pmid = 8760799 | pmc = 2192711 | doi = 10.1084/jem.184.2.457 }}</ref> * SHB,<ref name="pmid12084069">{{cite journal | vauthors = Lindholm CK, Henriksson ML, Hallberg B, Welsh M | title = Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells | journal = European Journal of Biochemistry | volume = 269 | issue = 13 | pages = 3279–3288 | date = July 2002 | pmid = 12084069 | doi = 10.1046/j.1432-1033.2002.03008.x | doi-access = }}</ref> and * VAV1.<ref name="pmid9047237">{{cite journal | vauthors = Raab M, da Silva AJ, Findell PR, Rudd CE | title = Regulation of Vav-SLP-76 binding by ZAP-70 and its relevance to TCR zeta/CD3 induction of interleukin-2 | journal = Immunity | volume = 6 | issue = 2 | pages = 155–164 | date = February 1997 | pmid = 9047237 | doi = 10.1016/S1074-7613(00)80422-7 | doi-access = free }}</ref><ref name="pmid8703037">{{cite journal | vauthors = Onodera H, Motto DG, Koretzky GA, Rothstein DM | title = Differential regulation of activation-induced tyrosine phosphorylation and recruitment of SLP-76 to Vav by distinct isoforms of the CD45 protein-tyrosine phosphatase | journal = The Journal of Biological Chemistry | volume = 271 | issue = 36 | pages = 22225–22230 | date = September 1996 | pmid = 8703037 | doi = 10.1074/jbc.271.36.22225 | doi-access = free }}</ref>
{{Div col end}}
== See also == * Activation
== References == {{Reflist}}
== Further reading == {{Refbegin| 2}} * {{cite journal | vauthors = Jackman JK, Motto DG, Sun Q, Tanemoto M, Turck CW, Peltz GA, Koretzky GA, Findell PR | display-authors = 6 | title = Molecular cloning of SLP-76, a 76-kDa tyrosine phosphoprotein associated with Grb2 in T cells | journal = The Journal of Biological Chemistry | volume = 270 | issue = 13 | pages = 7029–7032 | date = March 1995 | pmid = 7706237 | doi = 10.1074/jbc.270.13.7029 | doi-access = free }} * {{cite journal | vauthors = Sunden SL, Carr LL, Clements JL, Motto DG, Koretzky GA | title = Polymorphism in and localization of the gene LCP2 (SLP-76) to chromosome 5q33.1-qter | journal = Genomics | volume = 35 | issue = 1 | pages = 269–270 | date = July 1996 | pmid = 8661136 | doi = 10.1006/geno.1996.0354 }} * {{cite journal | vauthors = Motto DG, Ross SE, Wu J, Hendricks-Taylor LR, Koretzky GA | title = Implication of the GRB2-associated phosphoprotein SLP-76 in T cell receptor-mediated interleukin 2 production | journal = The Journal of Experimental Medicine | volume = 183 | issue = 4 | pages = 1937–1943 | date = April 1996 | pmid = 8666952 | pmc = 2192521 | doi = 10.1084/jem.183.4.1937 }} * {{cite journal | vauthors = Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR | display-authors = 6 | title = Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function | journal = The Journal of Biological Chemistry | volume = 271 | issue = 33 | pages = 19641–19644 | date = August 1996 | pmid = 8702662 | doi = 10.1074/jbc.271.33.19641 | doi-access = free }} * {{cite journal | vauthors = Onodera H, Motto DG, Koretzky GA, Rothstein DM | title = Differential regulation of activation-induced tyrosine phosphorylation and recruitment of SLP-76 to Vav by distinct isoforms of the CD45 protein-tyrosine phosphatase | journal = The Journal of Biological Chemistry | volume = 271 | issue = 36 | pages = 22225–22230 | date = September 1996 | pmid = 8703037 | doi = 10.1074/jbc.271.36.22225 | doi-access = free }} * {{cite journal | vauthors = Mizuno K, Katagiri T, Hasegawa K, Ogimoto M, Yakura H | title = Hematopoietic cell phosphatase, SHP-1, is constitutively associated with the SH2 domain-containing leukocyte protein, SLP-76, in B cells | journal = The Journal of Experimental Medicine | volume = 184 | issue = 2 | pages = 457–463 | date = August 1996 | pmid = 8760799 | pmc = 2192711 | doi = 10.1084/jem.184.2.457 }} * {{cite journal | vauthors = Raab M, da Silva AJ, Findell PR, Rudd CE | title = Regulation of Vav-SLP-76 binding by ZAP-70 and its relevance to TCR zeta/CD3 induction of interleukin-2 | journal = Immunity | volume = 6 | issue = 2 | pages = 155–164 | date = February 1997 | pmid = 9047237 | doi = 10.1016/S1074-7613(00)80422-7 | doi-access = free }} * {{cite journal | vauthors = Musci MA, Hendricks-Taylor LR, Motto DG, Paskind M, Kamens J, Turck CW, Koretzky GA | title = Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine kinases | journal = The Journal of Biological Chemistry | volume = 272 | issue = 18 | pages = 11674–11677 | date = May 1997 | pmid = 9115214 | doi = 10.1074/jbc.272.18.11674 | doi-access = free }} * {{cite journal | vauthors = da Silva AJ, Li Z, de Vera C, Canto E, Findell P, Rudd CE | title = Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 94 | issue = 14 | pages = 7493–7498 | date = July 1997 | pmid = 9207119 | pmc = 23849 | doi = 10.1073/pnas.94.14.7493 | doi-access = free | bibcode = 1997PNAS...94.7493D }} * {{cite journal | vauthors = Fu C, Chan AC | title = Identification of two tyrosine phosphoproteins, pp70 and pp68, which interact with phospholipase Cgamma, Grb2, and Vav after B cell antigen receptor activation | journal = The Journal of Biological Chemistry | volume = 272 | issue = 43 | pages = 27362–27368 | date = October 1997 | pmid = 9341187 | doi = 10.1074/jbc.272.43.27362 | doi-access = free }} * {{cite journal | vauthors = Zhang W, Sloan-Lancaster J, Kitchen J, Trible RP, Samelson LE | title = LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation | journal = Cell | volume = 92 | issue = 1 | pages = 83–92 | date = January 1998 | pmid = 9489702 | doi = 10.1016/S0092-8674(00)80901-0 | s2cid = 1806525 | doi-access = free }} * {{cite journal | vauthors = Fu C, Turck CW, Kurosaki T, Chan AC | title = BLNK: a central linker protein in B cell activation | journal = Immunity | volume = 9 | issue = 1 | pages = 93–103 | date = July 1998 | pmid = 9697839 | doi = 10.1016/S1074-7613(00)80591-9 | doi-access = free }} * {{cite journal | vauthors = Chu J, Liu Y, Koretzky GA, Durden DL | title = SLP-76-Cbl-Grb2-Shc interactions in FcgammaRI signaling | journal = Blood | volume = 92 | issue = 5 | pages = 1697–1706 | date = September 1998 | pmid = 9716598 | doi = 10.1182/blood.V92.5.1697 }} * {{cite journal | vauthors = Binstadt BA, Billadeau DD, Jevremović D, Williams BL, Fang N, Yi T, Koretzky GA, Abraham RT, Leibson PJ | display-authors = 6 | title = SLP-76 is a direct substrate of SHP-1 recruited to killer cell inhibitory receptors | journal = The Journal of Biological Chemistry | volume = 273 | issue = 42 | pages = 27518–27523 | date = October 1998 | pmid = 9765283 | doi = 10.1074/jbc.273.42.27518 | doi-access = free }} * {{cite journal | vauthors = Liu SK, Fang N, Koretzky GA, McGlade CJ | title = The hematopoietic-specific adaptor protein gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors | journal = Current Biology | volume = 9 | issue = 2 | pages = 67–75 | date = January 1999 | pmid = 10021361 | doi = 10.1016/S0960-9822(99)80017-7 | s2cid = 14131281 | doi-access = free | bibcode = 1999CBio....9...67L }} * {{cite journal | vauthors = Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP | display-authors = 6 | title = Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets | journal = The Journal of Biological Chemistry | volume = 274 | issue = 9 | pages = 5963–5971 | date = February 1999 | pmid = 10026222 | doi = 10.1074/jbc.274.9.5963 | doi-access = free }} * {{cite journal | vauthors = Erdreich-Epstein A, Liu M, Kant AM, Izadi KD, Nolta JA, Durden DL | title = Cbl functions downstream of Src kinases in Fc gamma RI signaling in primary human macrophages | journal = Journal of Leukocyte Biology | volume = 65 | issue = 4 | pages = 523–534 | date = April 1999 | pmid = 10204582 | doi = 10.1002/jlb.65.4.523 | s2cid = 18340540 }} * {{cite journal | vauthors = Asada H, Ishii N, Sasaki Y, Endo K, Kasai H, Tanaka N, Takeshita T, Tsuchiya S, Konno T, Sugamura K | display-authors = 6 | title = Grf40, A novel Grb2 family member, is involved in T cell signaling through interaction with SLP-76 and LAT | journal = The Journal of Experimental Medicine | volume = 189 | issue = 9 | pages = 1383–1390 | date = May 1999 | pmid = 10224278 | pmc = 2193052 | doi = 10.1084/jem.189.9.1383 }} * {{cite journal | vauthors = Wunderlich L, Faragó A, Downward J, Buday L | title = Association of Nck with tyrosine-phosphorylated SLP-76 in activated T lymphocytes | journal = European Journal of Immunology | volume = 29 | issue = 4 | pages = 1068–1075 | date = April 1999 | pmid = 10229072 | doi = 10.1002/(SICI)1521-4141(199904)29:04<1068::AID-IMMU1068>3.0.CO;2-P | doi-access = free }} * {{cite journal | vauthors = Gross BS, Melford SK, Watson SP | title = Evidence that phospholipase C-gamma2 interacts with SLP-76, Syk, Lyn, LAT and the Fc receptor gamma-chain after stimulation of the collagen receptor glycoprotein VI in human platelets | journal = European Journal of Biochemistry | volume = 263 | issue = 3 | pages = 612–623 | date = August 1999 | pmid = 10469124 | doi = 10.1046/j.1432-1327.1999.00560.x | doi-access = free }}
{{Refend}}
== External links == * {{MeshName|SLP-76+signal+Transducing+adaptor+proteins}}
Category:Proteins