词条 | Nesprin |
释义 |
| 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[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
References1. ^{{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 | pmid = 11792814 | doi = | url = http://jcs.biologists.org/cgi/content/abstract/114/24/4485 }} {{protein-stub}}2. ^1 2 {{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 }} 3. ^{{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 | url = https://www.ncbi.nlm.nih.gov/pubmed/?term=17158909 }} 4. ^1 2 {{cite journal | vauthors = Kumar A, Shivashankar GV | title = Dynamic interaction between actin and nesprin2 maintain the cell nucleus in a prestressed state | journal = Methods and Applications in Fluorescence | volume = 4 | issue = 4 | pages = 044008 | date = November 2016 | pmid = 28192301 | doi = 10.1088/2050-6120/4/4/044008 | url = https://doi.org/10.1088/2050-6120/4/4/044008 }} 5. ^{{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 | url = http://www.jcb.org/cgi/pmidlookup?view=long&pmid=16330710 | format = Free full text }} 6. ^{{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 | url = http://www.pnas.org/cgi/pmidlookup?view=long&pmid=19164528 | format = Free full text }} 7. ^{{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 }} 1 : Protein families |
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