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Volumn 80, Issue 1, 2014, Pages 193-204

Tracing the evolution of FERM domain of Kindlins

Author keywords

Evolutionary trace analysis; FERM domain; Focal adhesions; Kindlins; PH domain; Protein domain evolution

Indexed keywords

MEMBRANE PROTEIN;

EID: 84906731105     PISSN: 10557903     EISSN: 10959513     Source Type: Journal    
DOI: 10.1016/j.ympev.2014.08.008     Document Type: Article
Times cited : (41)

References (49)
  • 1
    • 65249107239 scopus 로고    scopus 로고
    • Simultaneous bayesian gene tree reconstruction and reconciliation analysis
    • Akerborg O., Sennblad B., Arvestad L., Lagergren J. Simultaneous bayesian gene tree reconstruction and reconciliation analysis. Proc. Natl. Acad. Sci. USA 2009, 106:5714-5719. 10.1073/pnas.0806251106.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5714-5719
    • Akerborg, O.1    Sennblad, B.2    Arvestad, L.3    Lagergren, J.4
  • 2
    • 0025183708 scopus 로고
    • Basic local alignment search tool
    • Altschul S., Gish W., Miller W., Myers E., Lipman D. Basic local alignment search tool. J. Mol. Biol. 1990, 215:403-410. http://dx.doi.org/10.1016/S0022-2836(05)80360-2.
    • (1990) J. Mol. Biol. , vol.215 , pp. 403-410
    • Altschul, S.1    Gish, W.2    Miller, W.3    Myers, E.4    Lipman, D.5
  • 3
    • 73649106911 scopus 로고    scopus 로고
    • Beta integrin tyrosine phosphorylation is a conserved mechanism for regulating Talin-induced integrin activation
    • Anthis N., Haling J., Oxley C., Memo M., Wegener K., Lim C., Ginsberg M., Campbell I. Beta integrin tyrosine phosphorylation is a conserved mechanism for regulating Talin-induced integrin activation. J. Biol. Chem. 2009, 284:36700-36710. 10.1074/jbc.M109.061275.
    • (2009) J. Biol. Chem. , vol.284 , pp. 36700-36710
    • Anthis, N.1    Haling, J.2    Oxley, C.3    Memo, M.4    Wegener, K.5    Lim, C.6    Ginsberg, M.7    Campbell, I.8
  • 5
    • 84859991132 scopus 로고    scopus 로고
    • Subcellular localization of Talin is regulated by inter-domain interactions
    • Banno A., Goult B., Lee H., Bate N., Critchley D., Ginsberg M. Subcellular localization of Talin is regulated by inter-domain interactions. J. Biol. Chem. 2012, 287:13799-13812. 10.1074/jbc.M112.341214.
    • (2012) J. Biol. Chem. , vol.287 , pp. 13799-13812
    • Banno, A.1    Goult, B.2    Lee, H.3    Bate, N.4    Critchley, D.5    Ginsberg, M.6
  • 7
    • 77952163960 scopus 로고    scopus 로고
    • Microtubule-mediated transport of the tumor-suppressor protein merlin and its mutants
    • Bensenor L., Barlan K., Rice S., Fehon R., Gelfand V. Microtubule-mediated transport of the tumor-suppressor protein merlin and its mutants. Proc. Natl. Acad. Sci. USA 2010, 107:7311-7316. 10.1073/pnas.0907389107.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 7311-7316
    • Bensenor, L.1    Barlan, K.2    Rice, S.3    Fehon, R.4    Gelfand, V.5
  • 10
  • 12
    • 84875214443 scopus 로고    scopus 로고
    • A feedback regulation between Kindlin-2 and GLI1 in prostate cancer cells
    • Gao J., Khan A., Shimokawa T., Zhan J., Stromblad S., Fang W., Zhang H. A feedback regulation between Kindlin-2 and GLI1 in prostate cancer cells. FEBS Lett. 2013, 587:631-638. 10.1016/j.febslet.2012.12.028.
    • (2013) FEBS Lett. , vol.587 , pp. 631-638
    • Gao, J.1    Khan, A.2    Shimokawa, T.3    Zhan, J.4    Stromblad, S.5    Fang, W.6    Zhang, H.7
  • 14
    • 46149093439 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of Talin in regulating integrin activation
    • Goksoy E., Ma Y., Wang X., Kong X., Perera D., Plow E., Qin J. Structural basis for the autoinhibition of Talin in regulating integrin activation. Mol. Cell. 2008, 31:124-133. 10.1016/j.molcel.2008.06.011.
    • (2008) Mol. Cell. , vol.31 , pp. 124-133
    • Goksoy, E.1    Ma, Y.2    Wang, X.3    Kong, X.4    Perera, D.5    Plow, E.6    Qin, J.7
  • 15
    • 0035798406 scopus 로고    scopus 로고
    • Assignment of homology to genome sequences using a library of hidden markov models that represent all proteins of known structure
    • Gough J., Karplus K., Hughey R., Chothia C. Assignment of homology to genome sequences using a library of hidden markov models that represent all proteins of known structure. J. Mol. Biol. 2001, 313:903-919. 10.1006/jmbi.2001.5080.
    • (2001) J. Mol. Biol. , vol.313 , pp. 903-919
    • Gough, J.1    Karplus, K.2    Hughey, R.3    Chothia, C.4
  • 16
    • 33744829519 scopus 로고    scopus 로고
    • An interaction between integrin and the Talin ferm domain mediates integrin activation but not linkage to the cytoskeleton
    • Guy Tanentzapf N.H.B. An interaction between integrin and the Talin ferm domain mediates integrin activation but not linkage to the cytoskeleton. Nat. Cell Biol. 2006, 1:601-606. . 10.1038/ncb1411.
    • (2006) Nat. Cell Biol. , vol.1 , pp. 601-606
    • Guy Tanentzapf, N.H.B.1
  • 17
    • 0034283003 scopus 로고    scopus 로고
    • Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain
    • Hamada K., Shimizu T., Matsui T., Tsukita S., Hakoshima T. Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J. 2000, 19:4449-4462. 10.1093/emboj/19.17.4449.
    • (2000) EMBO J. , vol.19 , pp. 4449-4462
    • Hamada, K.1    Shimizu, T.2    Matsui, T.3    Tsukita, S.4    Hakoshima, T.5
  • 18
    • 0033790239 scopus 로고    scopus 로고
    • Protein 4.1r core domain structure and insights into regulation of cytoskeletal organization
    • Han B., Nunomura W., Takakuwa Y., Mohandas N., Jap B. Protein 4.1r core domain structure and insights into regulation of cytoskeletal organization. Nat. Struct. Biol. 2000, 7:871-875. 10.1038/82819.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 871-875
    • Han, B.1    Nunomura, W.2    Takakuwa, Y.3    Mohandas, N.4    Jap, B.5
  • 19
    • 66449119343 scopus 로고    scopus 로고
    • Kindlin-1 and -2 directly bind the c-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects
    • Harburger D., Bouaouina M., Calderwood D. Kindlin-1 and -2 directly bind the c-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects. J. Biol. Chem. 2009, 284:11485-11497. 10.1074/jbc.M809233200.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11485-11497
    • Harburger, D.1    Bouaouina, M.2    Calderwood, D.3
  • 21
    • 33751381461 scopus 로고    scopus 로고
    • Timetree: a public knowledge-base of divergence times among organisms
    • Hedges S., Dudley J., Kumar S. Timetree: a public knowledge-base of divergence times among organisms. Bioinformatics 2006, 22:2971-2972. 10.1093/bioinformatics/btl505.
    • (2006) Bioinformatics , vol.22 , pp. 2971-2972
    • Hedges, S.1    Dudley, J.2    Kumar, S.3
  • 24
    • 79959277102 scopus 로고    scopus 로고
    • Phylogenetic analysis of Kindlins suggests subfunctionalization of an ancestral unduplicated Kindlin into three paralogs in vertebrates
    • Khan A., Janke A., Shimokawa T., Zhang H. Phylogenetic analysis of Kindlins suggests subfunctionalization of an ancestral unduplicated Kindlin into three paralogs in vertebrates. Evol. Bioinform. Online 2011, 7:7-19. 10.4137/EBO.S6179.
    • (2011) Evol. Bioinform. Online , vol.7 , pp. 7-19
    • Khan, A.1    Janke, A.2    Shimokawa, T.3    Zhang, H.4
  • 25
    • 84980115073 scopus 로고
    • Congenital poikiloderma with traumatic bulla formation and progressive cutaneous atrophy
    • Kindler T. Congenital poikiloderma with traumatic bulla formation and progressive cutaneous atrophy. Brit. J. Dermatol. 1954, 66:104-111.
    • (1954) Brit. J. Dermatol. , vol.66 , pp. 104-111
    • Kindler, T.1
  • 26
    • 77649181584 scopus 로고    scopus 로고
    • The role of Kindlins in cell biology and relevance to human disease
    • Lai-Cheong J., Parsons M., McGrath J. The role of Kindlins in cell biology and relevance to human disease. Int. J. Biochem. Cell Biol. 2010, 42:595-603. 10.1016/j.biocel.2009.10.015.
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 595-603
    • Lai-Cheong, J.1    Parsons, M.2    McGrath, J.3
  • 27
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge O., Bourne H., Cohen F. An evolutionary trace method defines binding surfaces common to protein families. J. Mol. Biol. 1996, 257:342-358. 10.1006/jmbi.1996.0167.
    • (1996) J. Mol. Biol. , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.2    Cohen, F.3
  • 28
    • 83355174039 scopus 로고    scopus 로고
    • Structural basis of phosphoinositide binding to Kindlin-2 protein pleckstrin homology domain in regulating integrin activation
    • Liu J., Fukuda K., Xu Z., Ma Y., Hirbawi J., Mao X., Wu C., Plow E., Qin J. Structural basis of phosphoinositide binding to Kindlin-2 protein pleckstrin homology domain in regulating integrin activation. J. Biol. Chem. 2011, 286:43334-43342. 10.1074/jbc.M111.295352.
    • (2011) J. Biol. Chem. , vol.286 , pp. 43334-43342
    • Liu, J.1    Fukuda, K.2    Xu, Z.3    Ma, Y.4    Hirbawi, J.5    Mao, X.6    Wu, C.7    Plow, E.8    Qin, J.9
  • 29
    • 84863477602 scopus 로고    scopus 로고
    • Crystal structure of Kindlin-2 PH domain reveals a conformational transition for its membrane anchoring and regulation of integrin activation
    • Liu Y., Zhu Y., Ye S., Zhang R. Crystal structure of Kindlin-2 PH domain reveals a conformational transition for its membrane anchoring and regulation of integrin activation. Protein Cell 2012, 3:434-440. 10.1007/s13238-012-2046-1.
    • (2012) Protein Cell , vol.3 , pp. 434-440
    • Liu, Y.1    Zhu, Y.2    Ye, S.3    Zhang, R.4
  • 30
    • 37249083542 scopus 로고    scopus 로고
    • Cell-matrix adhesion complexes: master control machinery of cell migration
    • Lock J., Wehrle-Haller B., Stromblad S. Cell-matrix adhesion complexes: master control machinery of cell migration. Semin. Cancer Biol. 2008, 18:65-76. 10.1016/j.semcancer.2007.10.001.
    • (2008) Semin. Cancer Biol. , vol.18 , pp. 65-76
    • Lock, J.1    Wehrle-Haller, B.2    Stromblad, S.3
  • 31
    • 78449311309 scopus 로고    scopus 로고
    • PyETV: a PyMOL evolutionary trace viewer to analyze functional site predictions in protein complexes
    • Lua R., Lichtarge O. PyETV: a PyMOL evolutionary trace viewer to analyze functional site predictions in protein complexes. Bioinformatics 2010, 26:2981-2982. 10.1093/bioinformatics/btq566.
    • (2010) Bioinformatics , vol.26 , pp. 2981-2982
    • Lua, R.1    Lichtarge, O.2
  • 33
    • 43149085289 scopus 로고    scopus 로고
    • Kindlin-2 (mig-2): a co-activator of beta3 integrins
    • Ma Y., Qin J., Wu C., Plow E. Kindlin-2 (mig-2): a co-activator of beta3 integrins. J. Cell Biol. 2008, 181:439-446. 10.1083/jcb.200710196.
    • (2008) J. Cell Biol. , vol.181 , pp. 439-446
    • Ma, Y.1    Qin, J.2    Wu, C.3    Plow, E.4
  • 34
    • 3242887157 scopus 로고    scopus 로고
    • CD-search: protein domain annotations on the fly
    • W327-31
    • Marchler-Bauer A., Bryant S. CD-search: protein domain annotations on the fly. Nucl. Acids Res. 2004, 32:W327-31. 10.1093/nar/gkh454.
    • (2004) Nucl. Acids Res. , vol.32
    • Marchler-Bauer, A.1    Bryant, S.2
  • 36
    • 0034632070 scopus 로고    scopus 로고
    • The UNC-112 gene in caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane
    • Rogalski T., Mullen G., Gilbert M., Williams B., Moerman D. The UNC-112 gene in caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane. J. Cell Biol. 2000, 150:253-264.
    • (2000) J. Cell Biol. , vol.150 , pp. 253-264
    • Rogalski, T.1    Mullen, G.2    Gilbert, M.3    Williams, B.4    Moerman, D.5
  • 37
    • 34547120497 scopus 로고    scopus 로고
    • The MIG-2/integrin interaction strengthens cell-matrix adhesion and modulates cell motility
    • Shi X., Ma Y., Tu Y., Chen K., Wu S., Fukuda K., Qin J., Plow E., Wu C. The MIG-2/integrin interaction strengthens cell-matrix adhesion and modulates cell motility. J. Biol. Chem. 2007, 282:20455-20466. 10.1074/jbc.M611680200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20455-20466
    • Shi, X.1    Ma, Y.2    Tu, Y.3    Chen, K.4    Wu, S.5    Fukuda, K.6    Qin, J.7    Plow, E.8    Wu, C.9
  • 38
    • 0037155867 scopus 로고    scopus 로고
    • Structural basis for neurofibromatosis type 2. Crystal structure of the merlin FERM domain
    • Shimizu T., Seto A., Maita N., Hamada K., Tsukita S., Tsukita S., Hakoshima T. Structural basis for neurofibromatosis type 2. Crystal structure of the merlin FERM domain. J. Biol. Chem. 2002, 277:10332-10336. 10.1074/jbc.M109979200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10332-10336
    • Shimizu, T.1    Seto, A.2    Maita, N.3    Hamada, K.4    Tsukita, S.5    Tsukita, S.6    Hakoshima, T.7
  • 40
    • 84869442139 scopus 로고    scopus 로고
    • DLRS: gene tree evolution in light of a species tree
    • Sjostrand J., Sennblad B., Arvestad L., Lagergren J. DLRS: gene tree evolution in light of a species tree. Bioinformatics 2012, 28:2994-2995. 10.1093/bioinformatics/bts548.
    • (2012) Bioinformatics , vol.28 , pp. 2994-2995
    • Sjostrand, J.1    Sennblad, B.2    Arvestad, L.3    Lagergren, J.4
  • 42
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K., Peterson D., Peterson N., Stecher G., Nei M., Kumar S. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol. 2011, 28:2731-2739. 10.1093/molbev/msr121.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 43
    • 33747877557 scopus 로고    scopus 로고
    • The Kindlins: subcellular localization and expression during murine development
    • Ussar S., Wang H., Linder S., Fassler R., Moser M. The Kindlins: subcellular localization and expression during murine development. Exp. Cell Res. 2006, 312:3142-3151. 10.1016/j.yexcr.2006.06.030.
    • (2006) Exp. Cell Res. , vol.312 , pp. 3142-3151
    • Ussar, S.1    Wang, H.2    Linder, S.3    Fassler, R.4    Moser, M.5
  • 44
    • 77955483193 scopus 로고    scopus 로고
    • Immunopathologies linked to integrin signalling
    • Wang H., Lim D., Rudd C. Immunopathologies linked to integrin signalling. Semin. Immunopathol. 2010, 32:173-182. 10.1007/s00281-010-0202-3.
    • (2010) Semin. Immunopathol. , vol.32 , pp. 173-182
    • Wang, H.1    Lim, D.2    Rudd, C.3
  • 45
    • 84857686971 scopus 로고    scopus 로고
    • Structure and function of focal adhesions
    • Wehrle-Haller B. Structure and function of focal adhesions. Curr. Opin. Cell Biol. 2012, 24:116-124. 10.1016/j.ceb.2011.11.001.
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 116-124
    • Wehrle-Haller, B.1
  • 46
    • 0037211938 scopus 로고    scopus 로고
    • Actin, microtubules and focal adhesion dynamics during cell migration
    • Wehrle-Haller B., Imhof B. Actin, microtubules and focal adhesion dynamics during cell migration. Int. J. Biochem. Cell Biol. 2003, 35:39-50.
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 39-50
    • Wehrle-Haller, B.1    Imhof, B.2
  • 47
    • 80051802621 scopus 로고    scopus 로고
    • Kindlin: helper, co-activator, or booster of Talin in integrin activation?
    • Ye F., Petrich B. Kindlin: helper, co-activator, or booster of Talin in integrin activation?. Curr. Opin. Hematol. 2011, 18:356-360. 10.1097/MOH.0b013e3283497f09.
    • (2011) Curr. Opin. Hematol. , vol.18 , pp. 356-360
    • Ye, F.1    Petrich, B.2
  • 48
    • 81755172093 scopus 로고    scopus 로고
    • Unfurling of the band 4.1, ezrin, radixin, moesin (FERM) domain of the merlin tumor suppressor
    • Yogesha S., Sharff A., Giovannini M., Bricogne G., Izard T. Unfurling of the band 4.1, ezrin, radixin, moesin (FERM) domain of the merlin tumor suppressor. Protein Sci. 2011, 20:2113-2120. 10.1002/pro.751.
    • (2011) Protein Sci. , vol.20 , pp. 2113-2120
    • Yogesha, S.1    Sharff, A.2    Giovannini, M.3    Bricogne, G.4    Izard, T.5


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