Filamin
Filamins are a class of proteins that hold two actin filaments at large angles.[1] Filamin protein in mammals is made up of an actin-binding domain at its N-terminus that is followed by 24 immunoglobulin-like repeat modules of roughly 95 amino acids. There are two hinge regions; between repeats 15-16 and 23-24. Filamin gets cleaved at these hinge regions to generate smaller fragments of the protein. Filamin has two actin-binding sites with a V-linkage between them, so that it cross-links actin filaments into a network with the filaments orientated almost at right angles to one another.[2]
Filamin proteins include:
Over-expression of FLNA stops the regeneration of bladder carcinoma (BC) cells, by inhibiting the cell cycle and inducing apoptosis of BC cells.[3] FLNA has also been shown to reduce the mobility and invasion abilities of BC cells.[3]
References
- ^ Murray JT, Campbell DG, Peggie M, Mora A, Alfonso M, Cohen P (December 2004). "Identification of filamin C as a new physiological substrate of PKBalpha using KESTREL". The Biochemical Journal. 384 (Pt 3): 489–94. doi:10.1042/BJ20041058. PMC 1134134. PMID 15461588.
- ^ Alberts, Bruce, author University of California, San Francisco, USA (2017-08-07). Molecular Biology of the Cell. ISBN 978-1-317-56374-7. OCLC 1001364893.
{{cite book}}:|last=has generic name (help)CS1 maint: multiple names: authors list (link) - ^ a b Wang Z, Li C, Jiang M, Chen J, Yang M, Pu J (February 2018). "Filamin A (FLNA) regulates autophagy of bladder carcinoma cell and affects its proliferation, invasion and metastasis". International Urology and Nephrology. 50 (2): 263–273. doi:10.1007/s11255-017-1772-y. PMID 29288417.
External links
- filamins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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