PTK2
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Proteinska tirozinska kinaza 2 | |||||||||||
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![]() PDB prikaz C-terminalnog FAT domena baziran na 1k04[1]. | |||||||||||
Dostupne strukture | |||||||||||
1K04, 1K05, 1MP8, 1OW6, 1OW7, 1OW8, 2ETM, 2IJM, 2RA7, 3B71, 3BZ3, 3PXK, 3S9O, 4EBV, 4EBW, 4GU6, 4GU9, 4I4E, 4I4F, 4K8A, 4K9Y, 4KAB, 4KAO, 4NY0 | |||||||||||
Identifikatori | |||||||||||
Simboli | PTK2; FADK; FAK; FAK1; FRNK; PPP1R71; p125FAK; pp125FAK | ||||||||||
Vanjski ID | OMIM: 600758 MGI: 95481 HomoloGene: 7314 GeneCards: PTK2 Gene | ||||||||||
EC broj | 2.7.10.2 | ||||||||||
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Pregled RNK izražavanja | |||||||||||
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podaci | |||||||||||
Ortolozi | |||||||||||
Vrsta | Čovek | Miš | |||||||||
Entrez | 5747 | 14083 | |||||||||
Ensembl | ENSG00000169398 | ENSMUSG00000022607 | |||||||||
UniProt | Q05397 | P34152 | |||||||||
Ref. Sekv. (iRNK) | NM_001199649 | NM_001130409 | |||||||||
Ref. Sekv. (protein) | NP_001186578 | NP_001123881 | |||||||||
Lokacija (UCSC) | Chr 8: 141.67 - 142.01 Mb | Chr 15: 73.21 - 73.42 Mb | |||||||||
PubMed pretraga | [1] | [2] |
PTK2 proteinska tirozinska kinaza 2 (PTK2, Fokalna adheziona kinaza, FAK), protein je koji je kod ljudi kodiran PTK2 genom.[2] PTK2 je fokalna proteinska kinaza koja učestvuje u ćelijskoj adheziji (vazivanje ćelija za njihovo okruženje) i procesu širenja ćelija (kretanju ćelija).[3] Poznato je da kad je FAK blokiran, ćelija raka dojke postaju u manjoj meri metastatične usled umanjene mobilnosti.[4]
Interakcije
PTK2 formira interakcije sa:
- BCAR1,[5][6][7][8][9][10]
- BMX,[11]
- CD61,[12][13]
- CRK,[6][14]
- DCC,[15]
- FYN,[16][17]
- GIT1,[18][19][20]
- GRB7,[21]
- Grb2,[7][14][16][22][23]
- IRS1[24] and
- ITGB5,[12]
- JAK2,[25][26]
- MAPK8IP3,[27]
- NCK1,[28][29]
- NCK2,[29]
- NEDD9,[30]
- NEO1,[15]
- P53,[31]
- PIK3R1,[32]
- PTEN,[33][34]
- PXN,[10][35][36][37][38][39][40][41][42][43]
- RB1CC1,[44]
- STAT1,[45]
- Src,[6][14][16][24][46][47]
- Syk,[13][48]
- TGFB1I1,[36][49][50]
- TLN1,[35][51] i
- TSC2.[52]
Povezano
Reference
- ↑ Arold, S. T.; Hoellerer, M. K.; Noble, M. E. (2002). „The structural basis of localization and signaling by the focal adhesion targeting domain”. Structure (London, England : 1993) 10 (3): 319–327. DOI:10.1016/S0969-2126(02)00717-7. PMID 12005431. edit
- ↑ André E, Becker-André M (January 1993). „Expression of an N-terminally truncated form of human focal adhesion kinase in brain”. Biochemical and Biophysical Research Communications 190 (1): 140–7. DOI:10.1006/bbrc.1993.1022. PMID 8422239.
- ↑ Blackshaw, S. E.; Dow, J. Kamal; Lackie, J. M. (1999). The dictionary of cell and molecular biology (3rd izd.). San Diego: Academic Press. ISBN 0-12-432565-3.
- ↑ Physorg:When cancer cells can't let go
- ↑ Salgia R, Pisick E, Sattler M, Li JL, Uemura N, Wong WK, Burky SA, Hirai H, Chen LB, Griffin JD (October 1996). „p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene”. J. Biol. Chem. 271 (41): 25198–203. DOI:10.1074/jbc.271.41.25198. PMID 8810278.
- ↑ 6,0 6,1 6,2 Hsia DA, Mitra SK, Hauck CR, Streblow DN, Nelson JA, Ilic D, Huang S, Li E, Nemerow GR, Leng J, Spencer KS, Cheresh DA, Schlaepfer DD (March 2003). „Differential regulation of cell motility and invasion by FAK”. J. Cell Biol. 160 (5): 753-67. DOI:10.1083/jcb.200212114. PMC 2173366. PMID 12615911.
- ↑ 7,0 7,1 Hildebrand JD, Taylor JM, Parsons JT (June 1996). „An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase”. Mol. Cell. Biol. 16 (6): 3169-78. PMC 231310. PMID 8649427.
- ↑ Chellaiah MA, Biswas RS, Yuen D, Alvarez UM, Hruska KA (December 2001). „Phosphatidylinositol 3,4,5-trisphosphate directs association of Src homology 2-containing signaling proteins with gelsolin”. J. Biol. Chem. 276 (50): 47434-44. DOI:10.1074/jbc.M107494200. PMID 11577104.
- ↑ Okabe S, Fukuda S, Broxmeyer HE (July 2002). „Activation of Wiskott-Aldrich syndrome protein and its association with other proteins by stromal cell-derived factor-1alpha is associated with cell migration in a T-lymphocyte line”. Exp. Hematol. 30 (7): 761–6. DOI:10.1016/s0301-472x(02)00823-8. PMID 12135674.
- ↑ 10,0 10,1 Wang JF, Park IW, Groopman JE (April 2000). „Stromal cell-derived factor-1alpha stimulates tyrosine phosphorylation of multiple focal adhesion proteins and induces migration of hematopoietic progenitor cells: roles of phosphoinositide-3 kinase and protein kinase C”. Blood 95 (8): 2505-13. PMID 10753828.
- ↑ Chen R, Kim O, Li M, Xiong X, Guan JL, Kung HJ, Chen H, Shimizu Y, Qiu Y (May 2001). „Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain”. Nat. Cell Biol. 3 (5): 439-44. DOI:10.1038/35074500. PMID 11331870.
- ↑ 12,0 12,1 Eliceiri BP, Puente XS, Hood JD, Stupack DG, Schlaepfer DD, Huang XZ, Sheppard D, Cheresh DA (April 2002). „Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling”. J. Cell Biol. 157 (1): 149-60. DOI:10.1083/jcb.200109079. PMC 2173263. PMID 11927607.
- ↑ 13,0 13,1 Chung J, Gao AG, Frazier WA (June 1997). „Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3”. J. Biol. Chem. 272 (23): 14740–6. DOI:10.1074/jbc.272.23.14740. PMID 9169439.
- ↑ 14,0 14,1 14,2 Angers-Loustau A, Côté JF, Charest A, Dowbenko D, Spencer S, Lasky LA, Tremblay ML (March 1999). „Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts”. J. Cell Biol. 144 (5): 1019-31. DOI:10.1083/jcb.144.5.1019. PMC 2148201. PMID 10085298.
- ↑ 15,0 15,1 Ren XR, Ming GL, Xie Y, Hong Y, Sun DM, Zhao ZQ, Feng Z, Wang Q, Shim S, Chen ZF, Song HJ, Mei L, Xiong WC (November 2004). „Focal adhesion kinase in netrin-1 signaling”. Nat. Neurosci. 7 (11): 1204-12. DOI:10.1038/nn1330. PMID 15494733.
- ↑ 16,0 16,1 16,2 Messina S, Onofri F, Bongiorno-Borbone L, Giovedì S, Valtorta F, Girault JA, Benfenati F (January 2003). „Specific interactions of neuronal focal adhesion kinase isoforms with Src kinases and amphiphysin”. J. Neurochem. 84 (2): 253-65. DOI:10.1046/j.1471-4159.2003.01519.x. PMID 12558988.
- ↑ Arold ST, Ulmer TS, Mulhern TD, Werner JM, Ladbury JE, Campbell ID, Noble ME (May 2001). „The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases”. J. Biol. Chem. 276 (20): 17199-205. DOI:10.1074/jbc.M011185200. PMID 11278857.
- ↑ Ko J, Kim S, Valtschanoff JG, Shin H, Lee JR, Sheng M, Premont RT, Weinberg RJ, Kim E (March 2003). „Interaction between liprin-alpha and GIT1 is required for AMPA receptor targeting”. J. Neurosci. 23 (5): 1667-77. PMID 12629171.
- ↑ Kim S, Ko J, Shin H, Lee JR, Lim C, Han JH, Altrock WD, Garner CC, Gundelfinger ED, Premont RT, Kaang BK, Kim E (February 2003). „The GIT family of proteins forms multimers and associates with the presynaptic cytomatrix protein Piccolo”. J. Biol. Chem. 278 (8): 6291-300. DOI:10.1074/jbc.M212287200. PMID 12473661.
- ↑ Zhao ZS, Manser E, Loo TH, Lim L (September 2000). „Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly”. Mol. Cell. Biol. 20 (17): 6354-63. DOI:10.1128/MCB.20.17.6354-6363.2000. PMC 86110. PMID 10938112.
- ↑ Han DC, Guan JL (August 1999). „Association of focal adhesion kinase with Grb7 and its role in cell migration”. J. Biol. Chem. 274 (34): 24425-30. DOI:10.1074/jbc.274.34.24425. PMID 10446223.
- ↑ Sieg DJ, Hauck CR, Ilic D, Klingbeil CK, Schaefer E, Damsky CH, Schlaepfer DD (May 2000). „FAK integrates growth-factor and integrin signals to promote cell migration”. Nat. Cell Biol. 2 (5): 249-56. DOI:10.1038/35010517. PMID 10806474.
- ↑ Arold ST, Hoellerer MK, Noble ME (March 2002). „The structural basis of localization and signaling by the focal adhesion targeting domain”. Structure 10 (3): 319–27. DOI:10.1016/s0969-2126(02)00717-7. PMID 12005431.
- ↑ 24,0 24,1 Lebrun P, Mothe-Satney I, Delahaye L, Van Obberghen E, Baron V (November 1998). „Insulin receptor substrate-1 as a signaling molecule for focal adhesion kinase pp125(FAK) and pp60(src)”. J. Biol. Chem. 273 (48): 32244-53. DOI:10.1074/jbc.273.48.32244. PMID 9822703.
- ↑ Zhu T, Goh EL, Lobie PE (April 1998). „Growth hormone stimulates the tyrosine phosphorylation and association of p125 focal adhesion kinase (FAK) with JAK2. Fak is not required for stat-mediated transcription”. J. Biol. Chem. 273 (17): 10682-9. DOI:10.1074/jbc.273.17.10682. PMID 9553131.
- ↑ Ryu H, Lee JH, Kim KS, Jeong SM, Kim PH, Chung HT (August 2000). „Regulation of neutrophil adhesion by pituitary growth hormone accompanies tyrosine phosphorylation of Jak2, p125FAK, and paxillin”. J. Immunol. 165 (4): 2116-23. DOI:10.4049/jimmunol.165.4.2116. PMID 10925297.
- ↑ Takino T, Yoshioka K, Miyamori H, Yamada KM, Sato H (September 2002). „A scaffold protein in the c-Jun N-terminal kinase signaling pathway is associated with focal adhesion kinase and tyrosine-phosphorylated”. Oncogene 21 (42): 6488-97. DOI:10.1038/sj.onc.1205840. PMID 12226752.
- ↑ Minegishi M, Tachibana K, Sato T, Iwata S, Nojima Y, Morimoto C (October 1996). „Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes”. J. Exp. Med. 184 (4): 1365-75. DOI:10.1084/jem.184.4.1365. PMC 2192828. PMID 8879209.
- ↑ 29,0 29,1 Goicoechea SM, Tu Y, Hua Y, Chen K, Shen TL, Guan JL, Wu C (July 2002). „Nck-2 interacts with focal adhesion kinase and modulates cell motility”. Int. J. Biochem. Cell Biol. 34 (7): 791–805. DOI:10.1016/s1357-2725(02)00002-x. PMID 11950595.
- ↑ Law SF, Estojak J, Wang B, Mysliwiec T, Kruh G, Golemis EA (July 1996). „Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae”. Mol. Cell. Biol. 16 (7): 3327-37. PMC 231327. PMID 8668148.
- ↑ Lim ST, Chen XL, Lim Y, Hanson DA, Vo TT, Howerton K, Larocque N, Fisher SJ, Schlaepfer DD, Ilic D (January 2008). „Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation”. Mol. Cell 29 (1): 9-22. DOI:10.1016/j.molcel.2007.11.031. PMC 2234035. PMID 18206965.
- ↑ Guinebault C, Payrastre B, Racaud-Sultan C, Mazarguil H, Breton M, Mauco G, Plantavid M, Chap H (May 1995). „Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85 alpha with actin filaments and focal adhesion kinase”. J. Cell Biol. 129 (3): 831–42. DOI:10.1083/jcb.129.3.831. PMC 2120444. PMID 7537275.
- ↑ Tamura M, Gu J, Danen EH, Takino T, Miyamoto S, Yamada KM (July 1999). „PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway”. J. Biol. Chem. 274 (29): 20693-703. DOI:10.1074/jbc.274.29.20693. PMID 10400703.
- ↑ Haier J, Nicolson GL (February 2002). „PTEN regulates tumor cell adhesion of colon carcinoma cells under dynamic conditions of fluid flow”. Oncogene 21 (9): 1450-60. DOI:10.1038/sj.onc.1205213. PMID 11857088.
- ↑ 35,0 35,1 Zheng C, Xing Z, Bian ZC, Guo C, Akbay A, Warner L, Guan JL (January 1998). „Differential regulation of Pyk2 and focal adhesion kinase (FAK). The C-terminal domain of FAK confers response to cell adhesion”. J. Biol. Chem. 273 (4): 2384–9. DOI:10.1074/jbc.273.4.2384. PMID 9442086.
- ↑ 36,0 36,1 Matsuya M, Sasaki H, Aoto H, Mitaka T, Nagura K, Ohba T, Ishino M, Takahashi S, Suzuki R, Sasaki T (January 1998). „Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions”. J. Biol. Chem. 273 (2): 1003-14. DOI:10.1074/jbc.273.2.1003. PMID 9422762.
- ↑ Kovacic-Milivojević B, Roediger F, Almeida EA, Damsky CH, Gardner DG, Ilić D (August 2001). „Focal adhesion kinase and p130Cas mediate both sarcomeric organization and activation of genes associated with cardiac myocyte hypertrophy”. Mol. Biol. Cell 12 (8): 2290–307. DOI:10.1091/mbc.12.8.2290. PMC 58595. PMID 11514617.
- ↑ Turner CE, Brown MC, Perrotta JA, Riedy MC, Nikolopoulos SN, McDonald AR, Bagrodia S, Thomas S, Leventhal PS (May 1999). „Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling”. J. Cell Biol. 145 (4): 851-63. DOI:10.1083/jcb.145.4.851. PMC 2133183. PMID 10330411.
- ↑ Liu S, Kiosses WB, Rose DM, Slepak M, Salgia R, Griffin JD, Turner CE, Schwartz MA, Ginsberg MH (June 2002). „A fragment of paxillin binds the alpha 4 integrin cytoplasmic domain (tail) and selectively inhibits alpha 4-mediated cell migration”. J. Biol. Chem. 277 (23): 20887-94. DOI:10.1074/jbc.M110928200. PMID 11919182.
- ↑ Mazaki Y, Hashimoto S, Sabe H (March 1997). „Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins”. J. Biol. Chem. 272 (11): 7437–44. DOI:10.1074/jbc.272.11.7437. PMID 9054445.
- ↑ Brown MC, Perrotta JA, Turner CE (November 1996). „Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding”. J. Cell Biol. 135 (4): 1109–23. DOI:10.1083/jcb.135.4.1109. PMC 2133378. PMID 8922390.
- ↑ Fujita H, Kamiguchi K, Cho D, Shibanuma M, Morimoto C, Tachibana K (October 1998). „Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase”. J. Biol. Chem. 273 (41): 26516–21. DOI:10.1074/jbc.273.41.26516. PMID 9756887.
- ↑ Zhang Z, Hernandez-Lagunas L, Horne WC, Baron R (August 1999). „Cytoskeleton-dependent tyrosine phosphorylation of the p130(Cas) family member HEF1 downstream of the G protein-coupled calcitonin receptor. Calcitonin induces the association of HEF1, paxillin, and focal adhesion kinase”. J. Biol. Chem. 274 (35): 25093-8. DOI:10.1074/jbc.274.35.25093. PMID 10455189.
- ↑ Ueda H, Abbi S, Zheng C, Guan JL (April 2000). „Suppression of Pyk2 kinase and cellular activities by FIP200”. J. Cell Biol. 149 (2): 423-30. DOI:10.1083/jcb.149.2.423. PMC 2175150. PMID 10769033.
- ↑ Xie B, Zhao J, Kitagawa M, Durbin J, Madri JA, Guan JL, Fu XY (June 2001). „Focal adhesion kinase activates Stat1 in integrin-mediated cell migration and adhesion”. J. Biol. Chem. 276 (22): 19512-23. DOI:10.1074/jbc.M009063200. PMID 11278462.
- ↑ Hecker TP, Grammer JR, Gillespie GY, Stewart J, Gladson CL (May 2002). „Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples”. Cancer Res. 62 (9): 2699-707. PMID 11980671.
- ↑ Relou IA, Bax LA, van Rijn HJ, Akkerman JW (January 2003). „Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein”. Biochem. J. 369 (Pt 2): 407-16. DOI:10.1042/BJ20020410. PMC 1223094. PMID 12387730.
- ↑ Sada K, Minami Y, Yamamura H (September 1997). „Relocation of Syk protein-tyrosine kinase to the actin filament network and subsequent association with Fak”. Eur. J. Biochem. 248 (3): 827–33. DOI:10.1111/j.1432-1033.1997.00827.x. PMID 9342235.
- ↑ Nishiya N, Tachibana K, Shibanuma M, Mashimo JI, Nose K (August 2001). „Hic-5-reduced cell spreading on fibronectin: competitive effects between paxillin and Hic-5 through interaction with focal adhesion kinase”. Mol. Cell. Biol. 21 (16): 5332-45. DOI:10.1128/MCB.21.16.5332-5345.2001. PMC 87257. PMID 11463817.
- ↑ Thomas SM, Hagel M, Turner CE (January 1999). „Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin”. J. Cell. Sci. 112 (2): 181-90. PMID 9858471.
- ↑ Chen HC, Appeddu PA, Parsons JT, Hildebrand JD, Schaller MD, Guan JL (July 1995). „Interaction of focal adhesion kinase with cytoskeletal protein talin”. J. Biol. Chem. 270 (28): 16995–9. DOI:10.1074/jbc.270.28.16995. PMID 7622520.
- ↑ Gan B, Yoo Y, Guan JL (December 2006). „Association of focal adhesion kinase with tuberous sclerosis complex 2 in the regulation of s6 kinase activation and cell growth”. J. Biol. Chem. 281 (49): 37321-9. DOI:10.1074/jbc.M605241200. PMID 17043358.
Literatura
- Iwata S, Ohashi Y, Kamiguchi K, Morimoto C (2000). „Beta 1-integrin-mediated cell signaling in T lymphocytes”. J. Dermatol. Sci. 23 (2): 75–86. DOI:10.1016/S0923-1811(99)00096-1. PMID 10808124.
- Schaller MD (2001). „Biochemical signals and biological responses elicited by the focal adhesion kinase”. Biochim. Biophys. Acta 1540 (1): 1–21. DOI:10.1016/S0167-4889(01)00123-9. PMID 11476890.
- Panetti TS (2002). „Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration”. Front. Biosci. 7: d143–50. DOI:10.2741/panetti. PMID 11779709.
- Hauck CR, Hsia DA, Schlaepfer DD (2003). „The focal adhesion kinase--a regulator of cell migration and invasion”. IUBMB Life 53 (2): 115–9. DOI:10.1080/15216540211470. PMID 12049193.
- Hanks SK, Ryzhova L, Shin NY, Brábek J (2004). „Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility”. Front. Biosci. 8: d982–96. DOI:10.2741/1114. PMID 12700132.
- Gabarra-Niecko V, Schaller MD, Dunty JM (2004). „FAK regulates biological processes important for the pathogenesis of cancer”. Cancer Metastasis Rev. 22 (4): 359–74. DOI:10.1023/A:1023725029589. PMID 12884911.
Vanjske veze
- MBInfo: FAK
- FAK Arhivirano 2011-07-22 na Wayback Machine-u Info with links in the Cell Migration Gateway Arhivirano 2014-12-11 na Wayback Machine-u
- MeSH protein, human PTK2 protein, human
- "Breaking down cancer’s wall of resistance" Arhivirano 2014-12-11 na Wayback Machine-u, by DR Nick Peel, Cancer Research UK, Science blog, August 2014
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