Biology:Nesprin

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Nesprin
Identifiers
SymbolNesprin
InterProIPR030265
Membranome123

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] Nesprin-3 binds to plectin, which is bound to the intermediate filaments,[4] while nesprin-4 interacts with kinesin-1.[5]

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.[6]

See also

  • SYNE1
  • SYNE2
  • Spectrin repeat containing nuclear envelope family member 3

References

  1. "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. December 2001. doi:10.1242/jcs.114.24.4485. PMID 11792814. http://jcs.biologists.org/cgi/content/abstract/114/24/4485. 
  2. 2.0 2.1 2.2 "Nesprins: from the nuclear envelope and beyond". Expert Reviews in Molecular Medicine 15: e5. July 2013. doi:10.1017/erm.2013.6. PMID 23830188. 
  3. "KASH-domain proteins in nuclear migration, anchorage and other processes". Journal of Cell Science 119 (Pt 24): 5021–9. December 2006. doi:10.1242/jcs.03295. PMID 17158909. 
  4. "Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin". The Journal of Cell Biology 171 (5): 799–810. December 2005. doi:10.1083/jcb.200506083. PMID 16330710. 
  5. "Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization". Proceedings of the National Academy of Sciences of the United States of America 106 (7): 2194–9. February 2009. doi:10.1073/pnas.0808602106. PMID 19164528. Bibcode2009PNAS..106.2194R. 
  6. "Cell Mechanosensitivity to Extremely Low-Magnitude Signals Is Enabled by a LINCed Nucleus". Stem Cells 33 (6): 2063–76. June 2015. doi:10.1002/stem.2004. PMID 25787126.