Biology:LIMS1

Generic protein structure example

LIM and senescent cell antigen-like-containing domain protein 1 is a protein that in humans is encoded by the LIMS1 gene.

Function

The protein encoded by this gene is an adaptor protein which contains five LIM domains, or double zinc fingers. The protein is likely involved in integrin signaling through its LIM domain-mediated interaction with integrin-linked kinase, found in focal adhesion plaques. It is also thought to act as a bridge linking integrin-linked kinase to NCK adaptor protein 2, which is involved in growth factor receptor kinase signaling pathways. Its localization to the periphery of spreading cells also suggests that this protein may play a role in integrin-mediated cell adhesion or spreading.

Interactions

LIMS1 has been shown to interact with Integrin-linked kinase and NCK2.

Further reading

• "Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways". Mol. Biol. Cell 9 (12): 3367–82. 1998. doi:10.1091/mbc.9.12.3367. PMID 9843575. 
• "Antigens recognized by autologous antibody in patients with renal-cell carcinoma". Int. J. Cancer 83 (4): 456–64. 1999. doi:10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5. PMID 10508479. 
• "Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain". J. Biol. Chem. 276 (7): 4932–9. 2001. doi:10.1074/jbc.M007632200. PMID 11078733. 
• "A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading". J. Cell Biol. 153 (3): 585–98. 2001. doi:10.1083/jcb.153.3.585. PMID 11331308. 
• "Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites". J. Cell Sci. 115 (Pt 24): 4777–86. 2002. doi:10.1242/jcs.00166. PMID 12432066. 
• "Identification of PINCH in Schwann cells and DRG neurons: shuttling and signaling after nerve injury". Glia 41 (3): 213–23. 2003. doi:10.1002/glia.10138. PMID 12528177. 
• "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. 2003. doi:10.1038/nbt810. PMID 12665801. 
• "Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling". Nat. Struct. Biol. 10 (7): 558–64. 2003. doi:10.1038/nsb938. PMID 12794636. 
• "PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival". J. Biol. Chem. 278 (51): 51324–33. 2003. doi:10.1074/jbc.M309122200. PMID 14551191. 
• "Thymosin beta4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair". Nature 432 (7016): 466–72. 2004. doi:10.1038/nature03000. PMID 15565145. 
• "High-throughput mapping of a dynamic signaling network in mammalian cells". Science 307 (5715): 1621–5. 2005. doi:10.1126/science.1105776. PMID 15761153. Bibcode: 2005Sci...307.1621B. 
• "The Ras suppressor Rsu-1 binds to the LIM 5 domain of the adaptor protein PINCH1 and participates in adhesion-related functions". Exp. Cell Res. 306 (1): 168–79. 2005. doi:10.1016/j.yexcr.2005.01.025. PMID 15878342. 
• "Molecular dissection of PINCH-1 reveals a mechanism of coupling and uncoupling of cell shape modulation and survival". J. Biol. Chem. 280 (30): 27631–7. 2005. doi:10.1074/jbc.M504189200. PMID 15941716. 
• "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.