Cinasa lligada a les integrines

cinasa lligada a les integrines
Estructures disponibles
PDB	Cerca ortòloga: PDBe RCSB
Llista de codis id de PDB
	4HI9, 2KBX, 3F6Q, 3IXE, 3KMU, 3KMW, 3REP, 4HI8
Identificadors
Àlies	ILK (HUGO), HEL-S-28, ILK-1, ILK-2, P59, p59integrin linked kinase
Identif. externs	OMIM: 602366 MGI: 1195267 HomoloGene: 3318 GeneCards: ILK OMA: ILK - orthologs
Localització del gen (humà)
	Cromosoma: 11 (humà)
Fi	6.610.874 bp
Localització del gen (ratolí)
	Cromosoma: 7 (ratolí)
Fi	105.392.132 bp
Patró d'expressió d'ARN
	Més explicacions
	body of uterus ; ; artèria poplítia; ; Tibial arteries ; ; artèria coronària dreta; ; muscle layer of sigmoid colon ; ; aorta toràcica ; ; aorta ascendent ; ; Descending thoracic aorta ; ; saphenous vein ; ; artèria coronària esquerra;
	Més explicacions
	úter; ; granulòcit; ; cordó umbilical; ; aorta ascendent ; ; nervi òptic; ; tunica media of zone of aorta ; ; genital tubercle ; ; tail of embryo ; ; coll uterí; ; efferent ductule ;
	Més referències a dades d'expressió
	Més referències a dades d'expressió
Ontologia genètica
Funció molecular	transferase activity ; unió de nucleòtids ; protein kinase activity ; SH3 domain binding ; kinase activity ; integrin binding ; protein serine/threonine kinase activity ; unió proteica ; unió d'ATP ; protein kinase binding ; signal transducer activity ;
Component cel·lular	cell projection ; membrana ; cell-cell junction ; membrana plasmàtica ; sarcòmer ; nucleoplasma ; dendritic shaft ; Unió cel·lular ; cos cel·lular neuronal ; terminal bouton ; axó ; costamere ; lamel·lipodi ; stress fiber ; citoplasma ; citosol ; focal adhesion ;
Procés biològic	fibroblast migration ; NEURONA ; negative regulation of smooth muscle cell proliferation ; neuron projection morphogenesis ; positive regulation of protein kinase B signaling ; regulation of actin cytoskeleton organization ; positive regulation of MAP kinase activity ; protein kinase B signaling ; protein heterooligomerization ; negative regulation of protein kinase activity ; fosforilació ; myelin assembly ; positive regulation of cell-matrix adhesion ; positive regulation of cell migration ; positive regulation of canonical Wnt signaling pathway ; Schwann cell development ; negative regulation of neural precursor cell proliferation ; outflow tract morphogenesis ; negative regulation of smooth muscle cell migration ; negative regulation of apoptotic process ; myelination in peripheral nervous system ; positive regulation of axonogenesis ; positive regulation of transcription, DNA-templated ; protein phosphorylation ; negative regulation of cardiac muscle cell apoptotic process ; branching involved in ureteric bud morphogenesis ; positive regulation of osteoblast differentiation ; positive regulation of dendrite morphogenesis ; cell projection organization ; positive regulation of myoblast differentiation ; peptidyl-serine phosphorylation ; establishment or maintenance of epithelial cell apical/basal polarity ; regulation of cell growth ; positive regulation of cell population proliferation ; positive regulation of BMP signaling pathway ; integrin-mediated signaling pathway ; substrate adhesion-dependent cell spreading ; positive regulation of phosphorylation ; cell-matrix adhesion ; proliferació cel·lular ; positive regulation of axon extension ; platelet aggregation ; nerve development ; positive regulation of MAPK cascade ; cell junction assembly ; MAPK cascade ; desenvolupament d'organisme multicel·lular ; supramolecular fiber organization ; tumor necrosis factor-mediated signaling pathway ; positive regulation of NIK/NF-kappaB signaling ;
	Fonts: Amigo / QuickGO
Ortòlegs
	3611
	16202
	ENSG00000166333
	ENSMUSG00000030890
	Q13418
	O55222
	NM_001014794; NM_001014795; NM_001278441; NM_001278442; NM_004517
	NM_001161724; NM_010562
	NP_001014794; NP_001014795; NP_001265370; NP_001265371; NP_004508
	NP_001155196; NP_034692
	Wikidata
Veure/Editar gen humà	Veure/Editar gen del ratolí

La cinasa lligada a les integrines (en anglès:Integrin linked quinase. ILK DKFZp686F1765; ILK-2, P59) és una proteïna de 59kDa. Des del seu descobriment, la ILK s'ha associat amb múltiples funcions cel·lulars, com la migració cel·lular, la proliferació cel·lular, les adhersions cèl·lulars, la transducció de senyals i contribueix a la regulació de l'òxid nítric, que actua sobre la fisiologia del vas sanguini.

La ILK es produeix de forma regular en la paret de les artèries sanes, però és absent en casos d'ateroesclerosi on es dificulta el flux sanguini per l'acumulació de greix i residus. ILK podria se la proteïna clau per dissenyar tractaments de la hipertensió arterial.

El 2008, ILK es va trobar que es localitza al centrosoma i regula l'organització del fus mitòtic.^[5]

Interaccions

La cinasa lligada a les integrines s'ha demostrat que interacciona amb LIMS1,^[6]^[7] AKT1,^[8]^[9]^[10]^[11] i ACP6.^[12]

Referències

↑ ^1,0 ^1,1 ^1,2 GRCh38: Ensembl release 89: ENSG00000166333 - Ensembl, May 2017
↑ ^2,0 ^2,1 ^2,2 GRCm38: Ensembl release 89: ENSMUSG00000030890 – Ensembl, May 2017
↑ «Human PubMed Reference:». National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ «Mouse PubMed Reference:». National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Fielding AB, Dobreva I, McDonald PC, Foster LJ, Dedhar S «Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization». J. Cell Biol., 180, 4, febrer 2008, pàg. 681–9. DOI: 10.1083/jcb.200710074. PMC: 2265580. PMID: 18283114.
↑ Tu, Y; Li F, Goicoechea S, Wu C «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, març 1999, pàg. 2425–34. PMC: 84035. PMID: 10022929.
↑ Zhang, Yongjun; Chen Ka, Guo Lida, Wu Chuanyue «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, octubre 2002, pàg. 38328–38. DOI: 10.1074/jbc.M205576200. PMID: 12167643.
↑ Barry, Fiona A; Gibbins Jonathan M «Protein kinase B is regulated in platelets by the collagen receptor glycoprotein VI». J. Biol. Chem., 277, 15, abril 2002, pàg. 12874–8. DOI: 10.1074/jbc.M200482200. PMID: 11825911.
↑ Delcommenne, M; Tan C, Gray V, Rue L, Woodgett J, Dedhar S «Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase». Proc. Natl. Acad. Sci. U.S.A., 95, 19, setembre 1998, pàg. 11211–6. DOI: 10.1073/pnas.95.19.11211. PMC: 21621. PMID: 9736715.
↑ Persad, S; Attwell S, Gray V, Mawji N, Deng J T, Leung D, Yan J, Sanghera J, Walsh M P, Dedhar S «Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343». J. Biol. Chem., 276, 29, juliol 2001, pàg. 27462–9. DOI: 10.1074/jbc.M102940200. PMID: 11313365.
↑ Leung-Hagesteijn, C; Mahendra A, Naruszewicz I, Hannigan G E «Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1». EMBO J., 20, 9, maig 2001, pàg. 2160–70. DOI: 10.1093/emboj/20.9.2160. PMC: 125446. PMID: 11331582.
↑ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel «Large-scale mapping of human protein–protein interactions by mass spectrometry». Mol. Syst. Biol., 3, 1, 2007, pàg. 89. DOI: 10.1038/msb4100134. PMC: 1847948. PMID: 17353931.

Marta Saura, Susana Márquez, Manuel Rodríguez Puyol, Beatriz Herranz y Carlos Zaragoza. "Integrin-Linked Kinase Regulates Vasomotor Function by Preventing Endothelial Nitric Oxide Synthase Uncoupling: Role in Atherosclerosis" Circulation Research, December 22, 2011[ http://www.agenciasinc.es/Noticias/Descubren-que-una-proteina-podria-ayudar-a-prevenir-enfermedades-vasculares Ateroesclerosi Notícies CSIC ]

Bibliografia

Dedhar S «Cell-substrate interactions and signaling through ILK». Curr. Opin. Cell Biol., 12, 2, 2000, pàg. 250–6. DOI: 10.1016/S0955-0674(99)00083-6. PMID: 10712922.
Persad S, Dedhar S «The role of integrin-linked kinase (ILK) in cancer progression». Cancer Metastasis Rev., 22, 4, 2004, pàg. 375–84. DOI: 10.1023/A:1023777013659. PMID: 12884912.
Srivastava D, Yu S «Stretching to meet needs: integrin-linked kinase and the cardiac pump». Genes Dev., 20, 17, 2006, pàg. 2327–31. DOI: 10.1101/gad.1472506. PMID: 16951248.
Hannigan GE, Leung-Hagesteijn C, Fitz-Gibbon L, et al. «Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase». Nature, 379, 6560, 1996, pàg. 91–6. DOI: 10.1038/379091a0. PMID: 8538749.
Hannigan GE, Bayani J, Weksberg R, et al. «Mapping of the gene encoding the integrin-linked kinase, ILK, to human chromosome 11p15.5-p15.4». Genomics, 42, 1, 1997, pàg. 177–9. DOI: 10.1006/geno.1997.4719. PMID: 9177792.
Li F, Liu J, Mayne R, Wu C «Identification and characterization of a mouse protein kinase that is highly homologous to human integrin-linked kinase». Biochim. Biophys. Acta, 1358, 3, 1997, pàg. 215–20. DOI: 10.1016/S0167-4889(97)00089-X. PMID: 9366252.
Delcommenne M, Tan C, Gray V, et al. «Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase». Proc. Natl. Acad. Sci. U.S.A., 95, 19, 1998, pàg. 11211–6. DOI: 10.1073/pnas.95.19.11211. PMC: 21621. PMID: 9736715.
Chung DH, Lee JI, Kook MC, et al. «ILK (beta1-integrin-linked protein kinase): a novel immunohistochemical marker for Ewing's sarcoma and primitive neuroectodermal tumour». Virchows Arch., 433, 2, 1998, pàg. 113–7. DOI: 10.1007/s004280050225. PMID: 9737788.
Tu Y, Li F, Goicoechea S, Wu C «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, 1999, pàg. 2425–34. PMC: 84035. PMID: 10022929.
Feng J, Ito M, Ichikawa K, et al. «Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase». J. Biol. Chem., 274, 52, 2000, pàg. 37385–90. DOI: 10.1074/jbc.274.52.37385. PMID: 10601309.
Janji B, Melchior C, Vallar L, Kieffer N «Cloning of an isoform of integrin-linked kinase (ILK) that is upregulated in HT-144 melanoma cells following TGF-beta1 stimulation». Oncogene, 19, 27, 2000, pàg. 3069–77. DOI: 10.1038/sj.onc.1203640. PMID: 10871859.
Velyvis A, Yang Y, Wu C, Qin J «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, 2001, pàg. 4932–9. DOI: 10.1074/jbc.M007632200. PMID: 11078733.
Matsumoto M, Ogawa W, Hino Y, et al. «Inhibition of insulin-induced activation of Akt by a kinase-deficient mutant of the epsilon isozyme of protein kinase C». J. Biol. Chem., 276, 17, 2001, pàg. 14400–6. DOI: 10.1074/jbc.M011093200. PMID: 11278835.
Nikolopoulos SN, Turner CE «Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions». J. Biol. Chem., 276, 26, 2001, pàg. 23499–505. DOI: 10.1074/jbc.M102163200. PMID: 11304546.
Persad S, Attwell S, Gray V, et al. «Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343». J. Biol. Chem., 276, 29, 2001, pàg. 27462–9. DOI: 10.1074/jbc.M102940200. PMID: 11313365.
Tu Y, Huang Y, Zhang Y, et al. «A New Focal Adhesion Protein That Interacts with Integrin-Linked Kinase and Regulates Cell Adhesion and Spreading». J. Cell Biol., 153, 3, 2001, pàg. 585–98. DOI: 10.1083/jcb.153.3.585. PMC: 2190577. PMID: 11331308.
Leung-Hagesteijn C, Mahendra A, Naruszewicz I, Hannigan GE «Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1». EMBO J., 20, 9, 2001, pàg. 2160–70. DOI: 10.1093/emboj/20.9.2160. PMC: 125446. PMID: 11331582.
Yamaji S, Suzuki A, Sugiyama Y, et al. «A Novel Integrin-Linked Kinase–Binding Protein, Affixin, Is Involved in the Early Stage of Cell–Substrate Interaction». J. Cell Biol., 153, 6, 2001, pàg. 1251–64. DOI: 10.1083/jcb.153.6.1251. PMC: 2192033. PMID: 11402068.
Chen R, Kim O, Yang J, et al. «Regulation of Akt/PKB activation by tyrosine phosphorylation». J. Biol. Chem., 276, 34, 2001, pàg. 31858–62. DOI: 10.1074/jbc.C100271200. PMID: 11445557.
Fielding A, Dobreva I, McDonald PC, et al. «Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization». J. Cell Biol., 180, 4, 2008, pàg. 681–9. DOI: 10.1083/jcb.200710074. PMC: 2265580. PMID: 18283114.

Vegeu també

[refGRCh38Ensembl-1] 1,0 ^1,1 ^1,2 GRCh38: Ensembl release 89: ENSG00000166333 - Ensembl, May 2017

[refGRCm38Ensembl-2] 2,0 ^2,1 ^2,2 GRCm38: Ensembl release 89: ENSMUSG00000030890 – Ensembl, May 2017

[3] «Human PubMed Reference:». National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] «Mouse PubMed Reference:». National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] Fielding AB, Dobreva I, McDonald PC, Foster LJ, Dedhar S «Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization». J. Cell Biol., 180, 4, febrer 2008, pàg. 681–9. DOI: 10.1083/jcb.200710074. PMC: 2265580. PMID: 18283114.

[pmid10022929-6] Tu, Y; Li F, Goicoechea S, Wu C «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, març 1999, pàg. 2425–34. PMC: 84035. PMID: 10022929.

[pmid12167643-7] Zhang, Yongjun; Chen Ka, Guo Lida, Wu Chuanyue «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, octubre 2002, pàg. 38328–38. DOI: 10.1074/jbc.M205576200. PMID: 12167643.

[pmid11825911-8] Barry, Fiona A; Gibbins Jonathan M «Protein kinase B is regulated in platelets by the collagen receptor glycoprotein VI». J. Biol. Chem., 277, 15, abril 2002, pàg. 12874–8. DOI: 10.1074/jbc.M200482200. PMID: 11825911.

[pmid9736715-9] Delcommenne, M; Tan C, Gray V, Rue L, Woodgett J, Dedhar S «Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase». Proc. Natl. Acad. Sci. U.S.A., 95, 19, setembre 1998, pàg. 11211–6. DOI: 10.1073/pnas.95.19.11211. PMC: 21621. PMID: 9736715.

[pmid11313365-10] Persad, S; Attwell S, Gray V, Mawji N, Deng J T, Leung D, Yan J, Sanghera J, Walsh M P, Dedhar S «Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343». J. Biol. Chem., 276, 29, juliol 2001, pàg. 27462–9. DOI: 10.1074/jbc.M102940200. PMID: 11313365.

[pmid11331582-11] Leung-Hagesteijn, C; Mahendra A, Naruszewicz I, Hannigan G E «Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1». EMBO J., 20, 9, maig 2001, pàg. 2160–70. DOI: 10.1093/emboj/20.9.2160. PMC: 125446. PMID: 11331582.

[pmid17353931-12] Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel «Large-scale mapping of human protein–protein interactions by mass spectrometry». Mol. Syst. Biol., 3, 1, 2007, pàg. 89. DOI: 10.1038/msb4100134. PMC: 1847948. PMID: 17353931.

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