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Volumn 349, Issue 4, 2005, Pages 861-871

The remarkable mechanical strength of polycystin-1 supports a direct role in mechanotransduction

Author keywords

AFM; Ig; PKD; Protein folding; TRP channel

Indexed keywords

CONNECTIN; IMMUNOGLOBULIN; MEMBRANE PROTEIN; POLYCYSTIN 1;

EID: 19444372522     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.04.008     Document Type: Article
Times cited : (98)

References (52)
  • 1
    • 0028278058 scopus 로고
    • The polycystic kidney-disease-1 gene encodes a 14-kb transcript and lies within a duplicated region on chromosome-16
    • C.J. Ward, B. Peral, J. Hughes, S. Thomas, V. Gamble, and A.B. MacCarthy The polycystic kidney-disease-1 gene encodes a 14-kb transcript and lies within a duplicated region on chromosome-16 Cell 77 1994 881 894
    • (1994) Cell , vol.77 , pp. 881-894
    • Ward, C.J.1    Peral, B.2    Hughes, J.3    Thomas, S.4    Gamble, V.5    MacCarthy, A.B.6
  • 3
    • 0036785149 scopus 로고    scopus 로고
    • The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia
    • B.K. Yoder, X.Y. Hou, and L.M. Guay-Woodford The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia J. Am. Soc. Nephrol. 13 2002 2508 2516
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 2508-2516
    • Yoder, B.K.1    Hou, X.Y.2    Guay-Woodford, L.M.3
  • 4
    • 0041520528 scopus 로고    scopus 로고
    • New TRP channels in hearing and mechanosensation
    • D.P. Corey New TRP channels in hearing and mechanosensation Neuron 39 2003 585 588
    • (2003) Neuron , vol.39 , pp. 585-588
    • Corey, D.P.1
  • 5
    • 0000901618 scopus 로고
    • Contributions to the knowledge of some glands and epithelium
    • K.W. Zimmerman Contributions to the knowledge of some glands and epithelium Arch Mikr Anat 52 1898 552 706
    • (1898) Arch Mikr Anat , vol.52 , pp. 552-706
    • Zimmerman, K.W.1
  • 6
    • 0029586470 scopus 로고
    • Primary cilia in normal and pathological tissues
    • D.N. Wheatley Primary cilia in normal and pathological tissues Pathobiology 63 1995 222 238
    • (1995) Pathobiology , vol.63 , pp. 222-238
    • Wheatley, D.N.1
  • 7
    • 0037317302 scopus 로고    scopus 로고
    • Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells
    • S.M. Nauli, F.J. Alenghat, Y. Luo, E. Williams, P. Vassilev, and X.G. Lil Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells Nature Genet. 33 2003 129 137
    • (2003) Nature Genet. , vol.33 , pp. 129-137
    • Nauli, S.M.1    Alenghat, F.J.2    Luo, Y.3    Williams, E.4    Vassilev, P.5    Lil, X.G.6
  • 8
    • 0035498717 scopus 로고    scopus 로고
    • Bending the MDCK cell primary cilium increases intracellular calcium
    • H.A. Praetorius, and K.R. Spring Bending the MDCK cell primary cilium increases intracellular calcium J. Membr. Biol. 184 2001 71 79
    • (2001) J. Membr. Biol. , vol.184 , pp. 71-79
    • Praetorius, H.A.1    Spring, K.R.2
  • 11
    • 0035834136 scopus 로고    scopus 로고
    • Cardiovascular, skeletal, and renal defects in mice with a targeted disruption of the Pkd1 gene
    • C. Boulter, S. Mulroy, S. Webb, S. Fleming, K. Brindle, and R. Sandford Cardiovascular, skeletal, and renal defects in mice with a targeted disruption of the Pkd1 gene Proc. Natl Acad. Sci. USA 98 2001 12174 12179
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12174-12179
    • Boulter, C.1    Mulroy, S.2    Webb, S.3    Fleming, S.4    Brindle, K.5    Sandford, R.6
  • 12
    • 0037292096 scopus 로고    scopus 로고
    • The renal pelvis: Machinery that concentrates urine in the papilla
    • T.M. Dwyer, and B. Schmidt-Nielsen The renal pelvis: machinery that concentrates urine in the papilla News Physiol. Sci. 18 2003 1 6
    • (2003) News Physiol. Sci. , vol.18 , pp. 1-6
    • Dwyer, T.M.1    Schmidt-Nielsen, B.2
  • 13
    • 0029069583 scopus 로고
    • The polycystic kidney-disease-1 (Pkd1) gene encodes a novel protein with multiple cell recognition domains
    • J. Hughes, C.J. Ward, B. Peral, R. Aspinwall, K. Clark, and J.L. Sanmillan The polycystic kidney-disease-1 (Pkd1) gene encodes a novel protein with multiple cell recognition domains Nature Genet. 10 1995 151 160
    • (1995) Nature Genet. , vol.10 , pp. 151-160
    • Hughes, J.1    Ward, C.J.2    Peral, B.3    Aspinwall, R.4    Clark, K.5    Sanmillan, J.L.6
  • 14
    • 9844245128 scopus 로고    scopus 로고
    • Comparative analysis of the polycystic kidney disease 1 (PKD1) gene reveals an integral membrane glycoprotein with multiple evolutionary conserved domains
    • R. Sandford, B. Sgotto, S. Aparicio, S. Brenner, M. Vaudin, and R.K. Wilson Comparative analysis of the polycystic kidney disease 1 (PKD1) gene reveals an integral membrane glycoprotein with multiple evolutionary conserved domains Hum. Mol. Genet. 6 1997 1483 1489
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1483-1489
    • Sandford, R.1    Sgotto, B.2    Aparicio, S.3    Brenner, S.4    Vaudin, M.5    Wilson, R.K.6
  • 15
    • 0033555277 scopus 로고    scopus 로고
    • The structure of a PKD domain from polycystin-1: Implications for polycystic kidney disease
    • M. Bycroft, A. Bateman, J. Clarke, S.J. Hamill, R. Sandford, R.L. Thomas, and C. Chothia The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease EMBO J. 18 1999 297 305
    • (1999) EMBO J. , vol.18 , pp. 297-305
    • Bycroft, M.1    Bateman, A.2    Clarke, J.3    Hamill, S.J.4    Sandford, R.5    Thomas, R.L.6    Chothia, C.7
  • 16
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • M.S.Z. Kellermayer, S.B. Smith, H.L. Granzier, and C. Bustamante Folding-unfolding transitions in single titin molecules characterized with laser tweezers Science 276 1997 1112 1116
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 17
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • M. Rief, M. Gautel, F. Oesterhelt, J.M. Fernandez, and H.E. Gaub Reversible unfolding of individual titin immunoglobulin domains by AFM Science 276 1997 1109 1112
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 18
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • A.F. Oberhauser, P.E. Marszalek, H.P. Erickson, and J.M. Fernandez The molecular elasticity of the extracellular matrix protein tenascin Nature 393 1998 181 185
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 19
    • 0038368702 scopus 로고    scopus 로고
    • Conformational analysis of native fibronectin by means of force spectroscopy
    • Y. Oberdorfer, H. Fuchs, and A. Janshoff Conformational analysis of native fibronectin by means of force spectroscopy Langmuir 16 2000 9955 9958
    • (2000) Langmuir , vol.16 , pp. 9955-9958
    • Oberdorfer, Y.1    Fuchs, H.2    Janshoff, A.3
  • 20
    • 0035852740 scopus 로고    scopus 로고
    • Forced unfolding modulated by disulfide bonds in the Ig domains of a cell adhesion molecule
    • P. Carl, C.H. Kwok, G. Manderson, D.W. Speicher, and D.E. Discher Forced unfolding modulated by disulfide bonds in the Ig domains of a cell adhesion molecule Proc. Natl Acad. Sci. USA 98 2001 1565 1570
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 1565-1570
    • Carl, P.1    Kwok, C.H.2    Manderson, G.3    Speicher, D.W.4    Discher, D.E.5
  • 21
    • 0036707999 scopus 로고    scopus 로고
    • Versatile cloning system for construction of multimeric proteins for use in atomic force microscopy
    • A. Steward, J.L. Toca-Herrera, and J. Clarke Versatile cloning system for construction of multimeric proteins for use in atomic force microscopy Protein Sci. 11 2002 2179 2183
    • (2002) Protein Sci. , vol.11 , pp. 2179-2183
    • Steward, A.1    Toca-Herrera, J.L.2    Clarke, J.3
  • 22
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • R.B. Best, B. Li, A. Steward, V. Daggett, and J. Clarke Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation Biophys. J. 81 2001 2344 2356
    • (2001) Biophys. J. , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 23
    • 0034984382 scopus 로고    scopus 로고
    • Mapping the folding pathway of an immunoglobulin domain: Structural detail from phi value analysis and movement of the transition state
    • S.B. Fowler, and J. Clarke Mapping the folding pathway of an immunoglobulin domain: structural detail from phi value analysis and movement of the transition state Structure 9 2001 355 366
    • (2001) Structure , vol.9 , pp. 355-366
    • Fowler, S.B.1    Clarke, J.2
  • 24
    • 3342993179 scopus 로고    scopus 로고
    • Atomic force microscopy: Mechanical unfolding of proteins
    • R. Rounsevell, J.R. Forman, and J. Clarke Atomic force microscopy: mechanical unfolding of proteins Methods 34 2004 100 111
    • (2004) Methods , vol.34 , pp. 100-111
    • Rounsevell, R.1    Forman, J.R.2    Clarke, J.3
  • 25
    • 0028077880 scopus 로고
    • Biochemical and structural applications of scanning force microscopy
    • C. Bustamante, D.A. Erie, and D. Keller Biochemical and structural applications of scanning force microscopy Curr. Opin. Struct. Biol. 4 1994 750 760
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 750-760
    • Bustamante, C.1    Erie, D.A.2    Keller, D.3
  • 27
    • 0042744701 scopus 로고    scopus 로고
    • Mechanical unfolding of a titin Ig domain: Structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations
    • R.B. Best, S.B. Fowler, J.L.T. Herrera, A. Steward, E. Paci, and J. Clarke Mechanical unfolding of a titin Ig domain: structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations J. Mol. Biol. 330 2003 867 877
    • (2003) J. Mol. Biol. , vol.330 , pp. 867-877
    • Best, R.B.1    Fowler, S.B.2    Herrera, J.L.T.3    Steward, A.4    Paci, E.5    Clarke, J.6
  • 28
    • 1642493664 scopus 로고    scopus 로고
    • Tuning the mechanical stability of fibronectin type III modules through sequence variations
    • D. Craig, M. Gao, K. Schulten, and V. Vogel Tuning the mechanical stability of fibronectin type III modules through sequence variations Structure 12 2004 21 30
    • (2004) Structure , vol.12 , pp. 21-30
    • Craig, D.1    Gao, M.2    Schulten, K.3    Vogel, V.4
  • 29
    • 0042561888 scopus 로고    scopus 로고
    • Solvent viscosity dependence of the folding rate of a small protein: Distributed computing study
    • B. Zagrovic, and V. Pande Solvent viscosity dependence of the folding rate of a small protein: distributed computing study J. Comput. Chem. 24 2003 1432 1436
    • (2003) J. Comput. Chem. , vol.24 , pp. 1432-1436
    • Zagrovic, B.1    Pande, V.2
  • 31
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and unfolding of single molecules of the giant muscle protein titin
    • L. Tskhovrebova, J. Trinick, J.A. Sleep, and R.M. Simmons Elasticity and unfolding of single molecules of the giant muscle protein titin Nature 387 1997 308 312
    • (1997) Nature , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 34
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • M. Rief, J. Pascual, M. Saraste, and H.E. Gaub Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles J. Mol. Biol. 286 1999 553 561
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 35
    • 0029665047 scopus 로고    scopus 로고
    • Mechanical unfolding of alpha(2)-macroglobulin molecules with atomic force microscope
    • K. Mitsui, M. Hara, and A. Ikai Mechanical unfolding of alpha(2)-macroglobulin molecules with atomic force microscope FEBS Letters 385 1996 29 33
    • (1996) FEBS Letters , vol.385 , pp. 29-33
    • Mitsui, K.1    Hara, M.2    Ikai, A.3
  • 37
    • 10044247452 scopus 로고    scopus 로고
    • Mechanical unfolding intermediates observed by single-molecule force spectroscopy in a fibronectin type III module
    • L. Li, H.H.L. Huang, C.L. Badilla, and J.M. Fernandez Mechanical unfolding intermediates observed by single-molecule force spectroscopy in a fibronectin type III module J. Mol. Biol. 345 2005 817 826
    • (2005) J. Mol. Biol. , vol.345 , pp. 817-826
    • Li, L.1    Huang, H.H.L.2    Badilla, C.L.3    Fernandez, J.M.4
  • 41
    • 0031848099 scopus 로고    scopus 로고
    • Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
    • H. Lu, B. Isralewitz, A. Krammer, V. Vogel, and K. Schulten Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation Biophys. J. 75 1998 662 671
    • (1998) Biophys. J. , vol.75 , pp. 662-671
    • Lu, H.1    Isralewitz, B.2    Krammer, A.3    Vogel, V.4    Schulten, K.5
  • 43
    • 0031767965 scopus 로고    scopus 로고
    • The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy
    • M. Rief, M. Gautel, A. Schemmel, and H.E. Gaub The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy Biophys. J. 75 1998 3008 3014
    • (1998) Biophys. J. , vol.75 , pp. 3008-3014
    • Rief, M.1    Gautel, M.2    Schemmel, A.3    Gaub, H.E.4
  • 44
    • 0033151955 scopus 로고    scopus 로고
    • Steered molecular dynamics simulations of force-induced protein domain unfolding
    • H. Lu, and K. Schulten Steered molecular dynamics simulations of force-induced protein domain unfolding Proteins: Struct. Funct. Genet. 35 1999 453 463
    • (1999) Proteins: Struct. Funct. Genet. , vol.35 , pp. 453-463
    • Lu, H.1    Schulten, K.2
  • 45
    • 0034612284 scopus 로고    scopus 로고
    • Unfolding proteins by external forces and temperature: The importance of topology and energetics
    • E. Paci, and M. Karplus Unfolding proteins by external forces and temperature: the importance of topology and energetics Proc. Natl Acad. Sci. USA 97 2000 6521 6526
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6521-6526
    • Paci, E.1    Karplus, M.2
  • 46
    • 0036774262 scopus 로고    scopus 로고
    • Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins
    • H. Jing, J. Takagi, J.H. Liu, S. Lindgren, R.G. Zhang, and A. Joachimiak Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins Structure 10 2002 1453 1464
    • (2002) Structure , vol.10 , pp. 1453-1464
    • Jing, H.1    Takagi, J.2    Liu, J.H.3    Lindgren, S.4    Zhang, R.G.5    Joachimiak, A.6
  • 47
    • 0034326319 scopus 로고    scopus 로고
    • Polycystin-1, the product of the polycystic kidney disease 1 gene, co-localizes with desmosomes in MDCK cells
    • M.S. Scheffers, P. van der Bent, F. Prins, L. Spruit, M.H. Breuning, and S.V. Litvinov Polycystin-1, the product of the polycystic kidney disease 1 gene, co-localizes with desmosomes in MDCK cells Hum. Mol. Genet. 9 2000 2743 2750
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2743-2750
    • Scheffers, M.S.1    Van Der Bent, P.2    Prins, F.3    Spruit, L.4    Breuning, M.H.5    Litvinov, S.V.6
  • 48
    • 0032831465 scopus 로고    scopus 로고
    • The PKD1 gene product, "polycystin-1", is a tyrosine-phosphorylated protein that colocalizes with alpha 2 beta 1-integrin in focal clusters in adherent renal epithelia
    • P.D. Wilson, L. Geng, X.H. Li, and C.R. Burrow The PKD1 gene product, "polycystin-1", is a tyrosine-phosphorylated protein that colocalizes with alpha 2 beta 1-integrin in focal clusters in adherent renal epithelia Lab. Invest. 79 1999 1311 1323
    • (1999) Lab. Invest. , vol.79 , pp. 1311-1323
    • Wilson, P.D.1    Geng, L.2    Li, X.H.3    Burrow, C.R.4
  • 49
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • C.N. Pace Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol. 131 1986 266 280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 51
    • 0000036869 scopus 로고    scopus 로고
    • Simulation of activation free energies in molecular systems
    • E. Neria, S. Fischer, and M. Karplus Simulation of activation free energies in molecular systems J. Chem. Phys. 105 1996 1902 1921
    • (1996) J. Chem. Phys. , vol.105 , pp. 1902-1921
    • Neria, E.1    Fischer, S.2    Karplus, M.3
  • 52
    • 0033135638 scopus 로고    scopus 로고
    • Effective energy function for proteins in solution
    • T. Lazaridis, and M. Karplus Effective energy function for proteins in solution Proteins 35 1999 133 152
    • (1999) Proteins , vol.35 , pp. 133-152
    • Lazaridis, T.1    Karplus, M.2


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