Nesprin

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The 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.[3][4] Nesprin-1 and -2 bind to the actin filaments.[5] Nesprin-3 binds to plectin, which is bound to the intermediate filaments,[6] while nesprin-4 interacts with kinesin-1.[7]

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.[8]

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References[edit]

  1. ^ http://jcs.biologists.org/cgi/content/abstract/114/24/4485
  2. ^ "Nesprins: from the nuclear envelope and beyond". Expert Reviews in Molecular Medicine. 15. doi:10.1017/erm.2013.6. 
  3. ^ Rajgor, Dipen; Shanahan, Catherine M. (2013). "Nesprins: from the nuclear envelope and beyond". Expert Reviews in Molecular Medicine. 15: e5. doi:10.1017/erm.2013.6. 
  4. ^ Wilhelmsen, Kevin; Ketema, Mirjam; Truong, Hoa; Sonnenberg, Arnoud (2006-12-15). "KASH-domain proteins in nuclear migration, anchorage and other processes". Journal of Cell Science. 119 (Pt 24): 5021–5029. doi:10.1242/jcs.03295. ISSN 0021-9533. PMID 17158909. 
  5. ^ Rajgor, Dipen; Shanahan, Catherine M. (2013). "Nesprins: from the nuclear envelope and beyond". Expert Reviews in Molecular Medicine. 15: e5. doi:10.1017/erm.2013.6. 
  6. ^ Wilhelmsen, K; Litjens, SH; Kuikman, I; Tshimbalanga, N; Janssen, H; Van Den Bout, I; Raymond, K; Sonnenberg, A (Dec 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. ISSN 0021-9525. PMC 2171291Freely accessible. PMID 16330710. 
  7. ^ Roux, KJ; Crisp, ML; Liu, Q; Kim, D; Kozlov, S; Stewart, CL; Burke, B (Feb 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. ISSN 0027-8424. PMC 2650131Freely accessible. PMID 19164528. 
  8. ^ Uzer; et al. (2015). "Cell mechanosensitivity to extremely low magnitude signals is enabled by a LINCed nucleus". Stem Cells. 33: 2063–76. doi:10.1002/stem.2004. PMC 4458857Freely accessible. PMID 25787126.