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Volumn 371, Issue 3, 2008, Pages 582-586

The actin binding protein, fesselin, is a member of the synaptopodin family

Author keywords

Actin binding protein; Actin polymerization; Ca2+ calmodulin regulation; Fesselin; Myopodin; Synaptopodin

Indexed keywords

ACTIN BINDING PROTEIN; COMPLEMENTARY DNA; FESSELIN; OLIGONUCLEOTIDE; SYNAPTOPODIN;

EID: 43549121436     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.04.134     Document Type: Article
Times cited : (9)

References (23)
  • 2
    • 0035960656 scopus 로고    scopus 로고
    • Fesselin, a synaptopodin-like protein, stimulates actin nucleation and polymerization
    • Beall B., and Chalovich J.M. Fesselin, a synaptopodin-like protein, stimulates actin nucleation and polymerization. Biochemistry 40 (2001) 14252-14259
    • (2001) Biochemistry , vol.40 , pp. 14252-14259
    • Beall, B.1    Chalovich, J.M.2
  • 3
    • 7244245361 scopus 로고    scopus 로고
    • 2+-calmodulin regulates fesselin-induced actin polymerization
    • 2+-calmodulin regulates fesselin-induced actin polymerization. Biochemistry 43 (2004) 13875-13882
    • (2004) Biochemistry , vol.43 , pp. 13875-13882
    • Schroeter, M.1    Chalovich, J.M.2
  • 4
    • 28444478088 scopus 로고    scopus 로고
    • Fesselin binds to actin and myosin and inhibits actin-activated ATPase activity
    • Schroeter M.M., and Chalovich J.M. Fesselin binds to actin and myosin and inhibits actin-activated ATPase activity. J. Muscle Res. Cell Motil. 26 (2005) 183-189
    • (2005) J. Muscle Res. Cell Motil. , vol.26 , pp. 183-189
    • Schroeter, M.M.1    Chalovich, J.M.2
  • 6
    • 33746053239 scopus 로고    scopus 로고
    • Smooth muscle alpha-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization
    • Pham M., and Chalovich J.M. Smooth muscle alpha-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization. J. Muscle Res. Cell Motil. 27 (2006) 45-51
    • (2006) J. Muscle Res. Cell Motil. , vol.27 , pp. 45-51
    • Pham, M.1    Chalovich, J.M.2
  • 7
    • 34948838466 scopus 로고    scopus 로고
    • Localization of the actin-binding protein fesselin in chicken smooth muscle
    • (Supplementary Abstract)
    • Schroeter M.M., Renegar R.H., Leinweber B.D., Zary J.T., and Chalovich J.M. Localization of the actin-binding protein fesselin in chicken smooth muscle. Biophys. J. (2007) 815 (Supplementary Abstract)
    • (2007) Biophys. J. , pp. 815
    • Schroeter, M.M.1    Renegar, R.H.2    Leinweber, B.D.3    Zary, J.T.4    Chalovich, J.M.5
  • 8
    • 0002830350 scopus 로고    scopus 로고
    • Introduction to actin and actin-binding proteins
    • Kreis T., and Vale R. (Eds), Oxford University Press, New York
    • Pollard T.D. Introduction to actin and actin-binding proteins. In: Kreis T., and Vale R. (Eds). Guidebook to the Cytoskeletal and Motor Proteins. second ed. (1999), Oxford University Press, New York 3-11
    • (1999) Guidebook to the Cytoskeletal and Motor Proteins. second ed. , pp. 3-11
    • Pollard, T.D.1
  • 9
    • 0030816323 scopus 로고    scopus 로고
    • Synaptopodin: an actin-associated protein in telencephalic dendrites and renal podocytes
    • Mundel P., Heid H.W., Mundel T.M., Krüger M., Reiser J., and Kriz W. Synaptopodin: an actin-associated protein in telencephalic dendrites and renal podocytes. J. Cell Biol. 139 (1997) 193-204
    • (1997) J. Cell Biol. , vol.139 , pp. 193-204
    • Mundel, P.1    Heid, H.W.2    Mundel, T.M.3    Krüger, M.4    Reiser, J.5    Kriz, W.6
  • 10
    • 0035851920 scopus 로고    scopus 로고
    • Differentiation- and stress-dependent nuclear cytoplasmatic redistribution of myopodin, a novel actin-bundling protein
    • Weins A., Schwarz K., Faul C., Barisoni L., Linke W.A., and Mundel P. Differentiation- and stress-dependent nuclear cytoplasmatic redistribution of myopodin, a novel actin-bundling protein. J. Cell Biol. 155 (2001) 393-404
    • (2001) J. Cell Biol. , vol.155 , pp. 393-404
    • Weins, A.1    Schwarz, K.2    Faul, C.3    Barisoni, L.4    Linke, W.A.5    Mundel, P.6
  • 11
    • 18244384042 scopus 로고    scopus 로고
    • Synaptopodin regulates the actin-bundling activity of alpha-actinin in an isoform-specific manner
    • Asanuma K., Kim K., Oh J., Giardino L., Chabanis S., Faul C., Reiser J., and Mundel P. Synaptopodin regulates the actin-bundling activity of alpha-actinin in an isoform-specific manner. J. Clin. Invest. 115 (2005) 1188-1198
    • (2005) J. Clin. Invest. , vol.115 , pp. 1188-1198
    • Asanuma, K.1    Kim, K.2    Oh, J.3    Giardino, L.4    Chabanis, S.5    Faul, C.6    Reiser, J.7    Mundel, P.8
  • 12
    • 36849051314 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent kinase II, and calcineurin regulate the intracellular trafficking of myopodin between the Z-disc and the nucleus of cardiac myocytes
    • 2+/calmodulin-dependent kinase II, and calcineurin regulate the intracellular trafficking of myopodin between the Z-disc and the nucleus of cardiac myocytes. Mol. Cell. Biol. 27 (2007) 8215-8227
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8215-8227
    • Faul, C.1    Dhume, A.2    Schecter, S.D.3    Mundel, P.4
  • 13
    • 0031563832 scopus 로고    scopus 로고
    • Rearrangements of the cytoskeleton and cell contacts induce process formation during differentiation of conditionally immortalized mouse podocyte cell lines
    • Mundel P., Reiser J., Zuniga Mejia Borga A., Pavenstadt H., Davidson G.R., Kriz W., and Zeller R. Rearrangements of the cytoskeleton and cell contacts induce process formation during differentiation of conditionally immortalized mouse podocyte cell lines. Exp. Cell Res. 236 (1997) 248-258
    • (1997) Exp. Cell Res. , vol.236 , pp. 248-258
    • Mundel, P.1    Reiser, J.2    Zuniga Mejia Borga, A.3    Pavenstadt, H.4    Davidson, G.R.5    Kriz, W.6    Zeller, R.7
  • 15
    • 0041854196 scopus 로고    scopus 로고
    • Tumor suppressor role for myopodin in bladder cancer: loss of nuclear expression of myopodin is cell-cycle dependent and predicts clinical outcome
    • Sanchez-Carbayo M., Schwarz K., Charytonowicz E., Cordon-Cardo C., and Mundel P. Tumor suppressor role for myopodin in bladder cancer: loss of nuclear expression of myopodin is cell-cycle dependent and predicts clinical outcome. Oncogene 22 (2003) 5298-5305
    • (2003) Oncogene , vol.22 , pp. 5298-5305
    • Sanchez-Carbayo, M.1    Schwarz, K.2    Charytonowicz, E.3    Cordon-Cardo, C.4    Mundel, P.5
  • 17
    • 0001433809 scopus 로고
    • Method for determination of the amino acid sequence in peptides
    • Edman P.A. Method for determination of the amino acid sequence in peptides. Acta Chem. Scan. 4 (1950) 283-293
    • (1950) Acta Chem. Scan. , vol.4 , pp. 283-293
    • Edman, P.A.1
  • 18
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 19
    • 0028207238 scopus 로고
    • An improved procedure for enzymatic digestion of polyvinylidene difluoride-bound proteins for internal sequence analysis
    • Fernandez J., Andrews L., and Mische S.M. An improved procedure for enzymatic digestion of polyvinylidene difluoride-bound proteins for internal sequence analysis. Anal. Biochem. 218 (1994) 112-117
    • (1994) Anal. Biochem. , vol.218 , pp. 112-117
    • Fernandez, J.1    Andrews, L.2    Mische, S.M.3
  • 20
    • 33846657665 scopus 로고    scopus 로고
    • Podocyte-associated proteins FAT, alpha-actinin-4 and filtrin are expressed in langerhans islets of the pancreas
    • Rinta-Valkama J., Palmen T., Lassila M., and Holthofer H. Podocyte-associated proteins FAT, alpha-actinin-4 and filtrin are expressed in langerhans islets of the pancreas. Mol. Cell. Biochem. 294 (2007) 117-125
    • (2007) Mol. Cell. Biochem. , vol.294 , pp. 117-125
    • Rinta-Valkama, J.1    Palmen, T.2    Lassila, M.3    Holthofer, H.4
  • 23
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay B.K., Williamson M.P., and Sudol M. The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14 (2000) 231-241
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.