LIMS1

LIM and senescent cell antigen-like domains 1
PDB rendering based on 1g47.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1G47​, 1NYP​, 1U5S​, 2COR​, 2D8X​, 2KBX​, 3F6Q​, 4HI8​, 4HI9​
Identifiers
Symbols	LIMS1 ; PINCH; PINCH-1; PINCH1
External IDs	OMIM: 602567 HomoloGene: 68428 GeneCards: LIMS1 Gene
Gene ontology Molecular function • protein binding • zinc ion binding • protein kinase binding Cellular component • cytosol • plasma membrane • cell-cell junction • focal adhesion • perinuclear region of cytoplasm Biological process • epithelial to mesenchymal transition • cell aging • positive regulation of gene expression • positive regulation of cell-substrate adhesion • cell junction assembly • positive regulation of GTPase activity • establishment of protein localization • negative regulation of transcription, DNA-templated • regulation of epithelial cell proliferation • positive regulation of focal adhesion assembly • cellular response to transforming growth factor beta stimulus • positive regulation of substrate adhesion-dependent cell spreading Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3987	110829
Ensembl	ENSG00000169756	ENSMUSG00000019920
UniProt	P48059	Q99JW4
RefSeq (mRNA)	NM_001193482	NM_001193303
RefSeq (protein)	NP_001180411	NP_001180232
Location (UCSC)	Chr 2: 108.53 – 108.69 Mb	Chr 10: 58.32 – 58.42 Mb
PubMed search

LIM and senescent cell antigen-like-containing domain protein 1 is a protein that in humans is encoded by the LIMS1 gene.^[1][2][3]

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.^[3]

Interactions

LIMS1 has been shown to interact with Integrin-linked kinase^[2][4] and NCK2.^[2][5]

References

1. Rearden A (Aug 1994). "A new LIM protein containing an autoepitope homologous to "senescent cell antigen"". Biochem. Biophys. Res. Commun. 201 (3): 1124–31. doi:10.1006/bbrc.1994.1822. PMID 7517666.
2. Tu Y, Li F, Goicoechea S, Wu C (Mar 1999). "The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells". Mol. Cell. Biol. 19 (3): 2425–34. doi:10.1128/mcb.19.3.2425. PMC 84035. PMID 10022929.
3. "Entrez Gene: LIMS1 LIM and senescent cell antigen-like domains 1".
4. Zhang Y, Chen K, Guo L, Wu C (Oct 2002). "Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration". J. Biol. Chem. 277 (41): 38328–38. doi:10.1074/jbc.M205576200. PMID 12167643.
5. Tu Y, Li F, Wu C (Dec 1998). "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. doi:10.1091/mbc.9.12.3367. PMC 25640. PMID 9843575.

Further reading

• Tu Y, Li F, Wu C (1998). "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. doi:10.1091/mbc.9.12.3367. PMC 25640. PMID 9843575.
• Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jäger D, Jäger E, Knuth A, Chen YT, Old LJ (1999). "Antigens recognized by autologous antibody in patients with renal-cell carcinoma". Int. J. Cancer 83 (4): 456–64. doi:10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5. PMID 10508479.
• Velyvis A, Yang Y, Wu C, Qin J (2001). "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. doi:10.1074/jbc.M007632200. PMID 11078733.
• Tu Y, Huang Y, Zhang Y, Hua Y, Wu C (2001). "A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading". J. Cell Biol. 153 (3): 585–98. doi:10.1083/jcb.153.3.585. PMC 2190577. PMID 11331308.
• Zhang Y, Chen K, Tu Y, Velyvis A, Yang Y, Qin J, Wu C (2002). "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. doi:10.1242/jcs.00166. PMID 12432066.
• Campana WM, Myers RR, Rearden A (2003). "Identification of PINCH in Schwann cells and DRG neurons: shuttling and signaling after nerve injury". Glia 41 (3): 213–23. doi:10.1002/glia.10138. PMID 12528177.
• Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
• Velyvis A, Vaynberg J, Yang Y, Vinogradova O, Zhang Y, Wu C, Qin J (2003). "Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling". Nat. Struct. Biol. 10 (7): 558–64. doi:10.1038/nsb938. PMID 12794636.
• Fukuda T, Chen K, Shi X, Wu C (2003). "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. doi:10.1074/jbc.M309122200. PMID 14551191.
• Bock-Marquette I, Saxena A, White MD, Dimaio JM, Srivastava D (2004). "Thymosin beta4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair". Nature 432 (7016): 466–72. doi:10.1038/nature03000. PMID 15565145.
• Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, Shinjo F, Liu Y, Dembowy J, Taylor IW, Luga V, Przulj N, Robinson M, Suzuki H, Hayashizaki Y, Jurisica I, Wrana JL (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153.
• Dougherty GW, Chopp T, Qi SM, Cutler ML (2005). "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. doi:10.1016/j.yexcr.2005.01.025. PMID 15878342.
• Xu Z, Fukuda T, Li Y, Zha X, Qin J, Wu C (2005). "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. doi:10.1074/jbc.M504189200. PMID 15941716.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.