Nesprin

{{Infobox protein family | Symbol = Nesprin | Name = Nesprin | image = | width = | caption = | InterPro= IPR030265 | SMART= | PROSITE = | SCOP = | TCDB = | OPM family= | OPM protein= | Pfam= | PDB= | Membranome superfamily= 123 }} '''Nesprins''' (nuclear envelope spectrin repeat proteins)<ref name="pmid11792814">{{cite journal | vauthors = Zhang Q, Skepper JN, Yang F, Davies JD, Hegyi L, Roberts RG, Weissberg PL, Ellis JA, Shanahan CM | title = Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues | journal = Journal of Cell Science | volume = 114 | issue = Pt 24 | pages = 4485–98 | date = December 2001 | doi = 10.1242/jcs.114.24.4485 | pmid = 11792814 | url = http://jcs.biologists.org/cgi/content/abstract/114/24/4485 | url-access = subscription }}</ref> are a family of proteins that are found primarily in the outer nuclear membrane, as well as other subcellular compartments.<ref name = "Rajgor_2013">{{cite journal | vauthors = Rajgor D, Shanahan CM | title = Nesprins: from the nuclear envelope and beyond | journal = Expert Reviews in Molecular Medicine | volume = 15 | pages = e5 | date = July 2013 | pmid = 23830188 | pmc = 3733404 | doi = 10.1017/erm.2013.6 }}</ref> They contain a C-terminal KASH transmembrane domain and are part of the LINC complex (Linker of Nucleoskeleton and Cytoskeleton) which is a protein network that associates the nuclear envelope (the membrane surrounding the nucleus) to the cytoskeleton, outside the nucleus, and the nuclear lamina, inside the nucleus.<ref name = "Rajgor_2013" /><ref>{{cite journal | vauthors = Wilhelmsen K, Ketema M, Truong H, Sonnenberg A | title = KASH-domain proteins in nuclear migration, anchorage and other processes | journal = Journal of Cell Science | volume = 119 | issue = Pt 24 | pages = 5021–9 | date = December 2006 | pmid = 17158909 | doi = 10.1242/jcs.03295 | doi-access = free }}</ref> Nesprin-1 and -2 bind to the actin filaments.<ref name = "Rajgor_2013" /> Nesprin-3 binds to plectin, which is bound to the intermediate filaments,<ref>{{cite journal | vauthors = Wilhelmsen K, Litjens SH, Kuikman I, Tshimbalanga N, Janssen H, van den Bout I, Raymond K, Sonnenberg A | title = Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin | journal = The Journal of Cell Biology | volume = 171 | issue = 5 | pages = 799–810 | date = December 2005 | pmid = 16330710 | pmc = 2171291 | doi = 10.1083/jcb.200506083 }}</ref> while nesprin-4 interacts with kinesin-1.<ref>{{cite journal | vauthors = Roux KJ, Crisp ML, Liu Q, Kim D, Kozlov S, Stewart CL, Burke B | title = Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 106 | issue = 7 | pages = 2194–9 | date = February 2009 | pmid = 19164528 | pmc = 2650131 | doi = 10.1073/pnas.0808602106 | bibcode = 2009PNAS..106.2194R | doi-access = free }}</ref>

Nesprin mediated connections to the cytoskeleton provides mechanosensory functions in cells, as the absence or disruption of Nesprin family members at the nuclear envelope interferes with the cell's ability to sense and respond to mechanical challenges.<ref>{{cite journal | vauthors = Uzer G, Thompson WR, Sen B, Xie Z, Yen SS, Miller S, Bas G, Styner M, Rubin CT, Judex S, Burridge K, Rubin J | display-authors = 6 | title = Cell Mechanosensitivity to Extremely Low-Magnitude Signals Is Enabled by a LINCed Nucleus | journal = Stem Cells | volume = 33 | issue = 6 | pages = 2063–76 | date = June 2015 | pmid = 25787126 | pmc = 4458857 | doi = 10.1002/stem.2004 }}</ref>

== References == {{reflist|32em}}

Category:Protein families