Nesprin

Nesprin
Identifiers
Symbol Nesprin
InterPro IPR030265
Membranome 123

Nesprins (nuclear envelope spectrin repeat proteins[1] are a family of proteins that are found primarily in the outer nuclear membrane, as well as other subcellular compartments.[2] 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.[2][3] Nesprin-1 and -2 bind to the actin filaments.[2][4] Using FRAP (Fluorescence recovery after photobleaching) and FCCS (Fluorescence cross-correlation spectroscopy), it has been shown that there is a dynamic connection between nesprin-2 and actin.[4] Nesprin-3 binds to plectin, which is bound to the intermediate filaments,[5] while nesprin-4 interacts with kinesin-1.[6]

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.[7] The connection between nesprin and actin stress fibers is necessary to maintain nuclear height in fibroblasts and thus may be a key regulator of nuclear mechanotransduction and gene expression program in cells.[4]

See also

References

  1. ↑ Zhang Q, Skepper JN, Yang F, Davies JD, Hegyi L, Roberts RG, Weissberg PL, Ellis JA, Shanahan CM (December 2001). "Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues". Journal of Cell Science. 114 (Pt 24): 4485–98. PMID 11792814.
  2. 1 2 3 Rajgor D, Shanahan CM (July 2013). "Nesprins: from the nuclear envelope and beyond". Expert Reviews in Molecular Medicine. 15: e5. doi:10.1017/erm.2013.6. PMC 3733404. PMID 23830188.
  3. ↑ Wilhelmsen K, Ketema M, Truong H, Sonnenberg A (December 2006). "KASH-domain proteins in nuclear migration, anchorage and other processes". Journal of Cell Science. 119 (Pt 24): 5021–9. doi:10.1242/jcs.03295. PMID 17158909.
  4. 1 2 3 Kumar A, Shivashankar GV (November 2016). "Dynamic interaction between actin and nesprin2 maintain the cell nucleus in a prestressed state". Methods and Applications in Fluorescence. 4 (4): 044008. doi:10.1088/2050-6120/4/4/044008. PMID 28192301.
  5. ↑ Wilhelmsen K, Litjens SH, Kuikman I, Tshimbalanga N, Janssen H, van den Bout I, Raymond K, Sonnenberg A (December 2005). "Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin" (Free full text). The Journal of Cell Biology. 171 (5): 799–810. doi:10.1083/jcb.200506083. PMC 2171291. PMID 16330710.
  6. ↑ Roux KJ, Crisp ML, Liu Q, Kim D, Kozlov S, Stewart CL, Burke B (February 2009). "Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization" (Free full text). Proceedings of the National Academy of Sciences of the United States of America. 106 (7): 2194–9. doi:10.1073/pnas.0808602106. PMC 2650131. PMID 19164528.
  7. ↑ Uzer G, Thompson WR, Sen B, Xie Z, Yen SS, Miller S, et al. (June 2015). "Cell Mechanosensitivity to Extremely Low-Magnitude Signals Is Enabled by a LINCed Nucleus". Stem Cells. 33 (6): 2063–76. doi:10.1002/stem.2004. PMC 4458857. PMID 25787126.
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