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Volumn 4, Issue 7, 2009, Pages

Pyrin modulates the intracellular distribution of PSTPIP1

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOTIC SPECK PROTEIN; BINDING PROTEIN; CYCLIN DEPENDENT KINASE INHIBITOR; CYCLIN DEPENDENT KINASE INHIBITOR 4; MEMBRANE PROTEIN; PROLINE SERINE THREONINE PHOSPHATASE INTERACTING PROTEIN 1; PROTEIN; PROTEIN BAR; PROTEIN KINASE FES; PROTEIN SH3; PYRIN; TUBULIN; UNCLASSIFIED DRUG; CYTOSKELETON PROTEIN; MARENOSTRIN; PSTPIP1 PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 67650222428     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0006147     Document Type: Article
Times cited : (47)

References (37)
  • 2
    • 0030745449 scopus 로고    scopus 로고
    • Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever. The International FMF Consortium. Cell 90: 797-807
    • Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever. The International FMF Consortium. Cell 90: 797-807.
  • 3
    • 16944365196 scopus 로고    scopus 로고
    • A candidate gene for familial Mediterranean fever. The French FMF Consortium. Nat Genet 17: 25-31.
    • A candidate gene for familial Mediterranean fever. The French FMF Consortium. Nat Genet 17: 25-31.
  • 5
    • 0344823965 scopus 로고    scopus 로고
    • Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial Mediterranean fever and PAPA syndrome as disorders in the same pathway
    • Shoham NG, Centola M, Mansfield E, Hull KM, Wood G, et al. (2003) Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial Mediterranean fever and PAPA syndrome as disorders in the same pathway. Proc Natl Acad Sci U S A 100: 13501-13506.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 13501-13506
    • Shoham, N.G.1    Centola, M.2    Mansfield, E.3    Hull, K.M.4    Wood, G.5
  • 6
    • 0037091012 scopus 로고    scopus 로고
    • Mutations in CD2BP1 disrupt binding to PTP PEST and are responsible for PAPA syndrome, an autoinflammatory disorder
    • Wise CA, Gillum JD, Seidman CE, Lindor NM, Veile R, et al. (2002) Mutations in CD2BP1 disrupt binding to PTP PEST and are responsible for PAPA syndrome, an autoinflammatory disorder. Hum Mol Genet 11: 961-969.
    • (2002) Hum Mol Genet , vol.11 , pp. 961-969
    • Wise, C.A.1    Gillum, J.D.2    Seidman, C.E.3    Lindor, N.M.4    Veile, R.5
  • 7
    • 0032515158 scopus 로고    scopus 로고
    • A novel macrophage actin-associated protein (MAYP) is tyrosine-phosphorylated following colony stimulating factor-1 stimulation
    • Yeung YG, Soldera S, Stanley ER (1998) A novel macrophage actin-associated protein (MAYP) is tyrosine-phosphorylated following colony stimulating factor-1 stimulation. J Biol Chem 273: 30638-30642.
    • (1998) J Biol Chem , vol.273 , pp. 30638-30642
    • Yeung, Y.G.1    Soldera, S.2    Stanley, E.R.3
  • 8
    • 0032515170 scopus 로고    scopus 로고
    • PSTPIP 2, a second tyrosine phosphorylated, cytoskeletal-associated protein that binds a PEST-type protein-tyrosine phosphatase
    • Wu Y, Dowbenko D, Lasky LA (1998) PSTPIP 2, a second tyrosine phosphorylated, cytoskeletal-associated protein that binds a PEST-type protein-tyrosine phosphatase. J Biol Chem 273: 30487-30496.
    • (1998) J Biol Chem , vol.273 , pp. 30487-30496
    • Wu, Y.1    Dowbenko, D.2    Lasky, L.A.3
  • 9
    • 85047695184 scopus 로고    scopus 로고
    • Chronic recurrent multifocal osteomyelitis (CRMO): Evidence for a susceptibility gene located on chromosome 18q21.3-18q22
    • Golla A, Jansson A, Ramser J, Hellebrand H, Zahn R, et al. (2002) Chronic recurrent multifocal osteomyelitis (CRMO): evidence for a susceptibility gene located on chromosome 18q21.3-18q22. Eur J Hum Genet 10: 217-221.
    • (2002) Eur J Hum Genet , vol.10 , pp. 217-221
    • Golla, A.1    Jansson, A.2    Ramser, J.3    Hellebrand, H.4    Zahn, R.5
  • 10
    • 33645734214 scopus 로고    scopus 로고
    • Mutation of mouse Mayp/Pstpip2 causes a macrophage autoinflammatory disease
    • Grosse J, Chitu V, Marquardt A, Hanke P, Schmittwolf C, et al. (2006) Mutation of mouse Mayp/Pstpip2 causes a macrophage autoinflammatory disease. Blood 107: 3350-3358.
    • (2006) Blood , vol.107 , pp. 3350-3358
    • Grosse, J.1    Chitu, V.2    Marquardt, A.3    Hanke, P.4    Schmittwolf, C.5
  • 11
    • 29344448820 scopus 로고    scopus 로고
    • A missense mutation in pstpip2 is associated with the murine autoinflammatory disorder chronic multifocal osteomyelitis
    • Ferguson PJ, Bing X, Vasef MA, Ochoa LA, Mahgoub A, et al. (2006) A missense mutation in pstpip2 is associated with the murine autoinflammatory disorder chronic multifocal osteomyelitis. Bone 38: 41-47.
    • (2006) Bone , vol.38 , pp. 41-47
    • Ferguson, P.J.1    Bing, X.2    Vasef, M.A.3    Ochoa, L.A.4    Mahgoub, A.5
  • 12
    • 0034510155 scopus 로고    scopus 로고
    • Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation
    • Cong F, Spencer S, Cote JF, Wu Y, Tremblay ML, et al. (2000) Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation. Mol Cell 6: 1413-1423.
    • (2000) Mol Cell , vol.6 , pp. 1413-1423
    • Cong, F.1    Spencer, S.2    Cote, J.F.3    Wu, Y.4    Tremblay, M.L.5
  • 13
    • 0032489515 scopus 로고    scopus 로고
    • Tyrosine phosphorylation regulates the SH3-mediated binding of the Wiskott-Aldrich syndrome protein to PSTPIP, a cytoskeletal-associated protein
    • Wu Y, Spencer SD, Lasky LA (1998) Tyrosine phosphorylation regulates the SH3-mediated binding of the Wiskott-Aldrich syndrome protein to PSTPIP, a cytoskeletal-associated protein. J Biol Chem 273: 5765-5770.
    • (1998) J Biol Chem , vol.273 , pp. 5765-5770
    • Wu, Y.1    Spencer, S.D.2    Lasky, L.A.3
  • 14
    • 0034677932 scopus 로고    scopus 로고
    • Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules
    • Tian L, Nelson DL, Stewart DM (2000) Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules. J Biol Chem 275: 7854-7861.
    • (2000) J Biol Chem , vol.275 , pp. 7854-7861
    • Tian, L.1    Nelson, D.L.2    Stewart, D.M.3
  • 15
    • 33748964289 scopus 로고    scopus 로고
    • Bar domain proteins: A role in tubulation, scission and actin assembly in clathrin-mediated endocytosis
    • Dawson JC, Legg JA, Machesky LM (2006) Bar domain proteins: a role in tubulation, scission and actin assembly in clathrin-mediated endocytosis. Trends Cell Biol 16: 493-498.
    • (2006) Trends Cell Biol , vol.16 , pp. 493-498
    • Dawson, J.C.1    Legg, J.A.2    Machesky, L.M.3
  • 16
    • 35348934890 scopus 로고    scopus 로고
    • Pyrin activates the ASC pyroptosome in response to engagement by autoinflammatory PSTPIP1 mutants
    • Yu JW, Fernandes-Alnemri T, Datta P, Wu J, Juliana C, et al. (2007) Pyrin activates the ASC pyroptosome in response to engagement by autoinflammatory PSTPIP1 mutants. Mol Cell 28: 214-227.
    • (2007) Mol Cell , vol.28 , pp. 214-227
    • Yu, J.W.1    Fernandes-Alnemri, T.2    Datta, P.3    Wu, J.4    Juliana, C.5
  • 17
    • 34447256592 scopus 로고    scopus 로고
    • Structure and analysis of FCHo2 F-BAR domain: A dimerizing and membrane recruitment module that effects membrane curvature
    • Henne WM, Kent HM, Ford MG, Hegde BG, Daumke O, et al. (2007) Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature. Structure 15: 839-852.
    • (2007) Structure , vol.15 , pp. 839-852
    • Henne, W.M.1    Kent, H.M.2    Ford, M.G.3    Hegde, B.G.4    Daumke, O.5
  • 18
    • 34249316521 scopus 로고    scopus 로고
    • Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis
    • Shimada A, Niwa H, Tsujita K, Suetsugu S, Nitta K, et al. (2007) Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis. Cell 129: 761-772.
    • (2007) Cell , vol.129 , pp. 761-772
    • Shimada, A.1    Niwa, H.2    Tsujita, K.3    Suetsugu, S.4    Nitta, K.5
  • 19
    • 30944435279 scopus 로고    scopus 로고
    • Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis
    • Tsujita K, Suetsugu S, Sasaki N, Furutani M, Oikawa T, et al. (2006) Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J Cell Biol 172: 269-279.
    • (2006) J Cell Biol , vol.172 , pp. 269-279
    • Tsujita, K.1    Suetsugu, S.2    Sasaki, N.3    Furutani, M.4    Oikawa, T.5
  • 20
    • 28444452974 scopus 로고    scopus 로고
    • Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins
    • Itoh T, Erdmann KS, Roux A, Habermann B, Werner H, et al. (2005) Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev Cell 9: 791-804.
    • (2005) Dev Cell , vol.9 , pp. 791-804
    • Itoh, T.1    Erdmann, K.S.2    Roux, A.3    Habermann, B.4    Werner, H.5
  • 21
    • 4544251239 scopus 로고    scopus 로고
    • A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis
    • Kamioka Y, Fukuhara S, Sawa H, Nagashima K, Masuda M, et al. (2004) A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis. J Biol Chem 279: 40091-40099.
    • (2004) J Biol Chem , vol.279 , pp. 40091-40099
    • Kamioka, Y.1    Fukuhara, S.2    Sawa, H.3    Nagashima, K.4    Masuda, M.5
  • 22
    • 0034620559 scopus 로고    scopus 로고
    • Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase
    • Jez JM, Ferrer JL, Bowman ME, Dixon RA, Noel JP (2000) Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase. Biochemistry 39: 890-902.
    • (2000) Biochemistry , vol.39 , pp. 890-902
    • Jez, J.M.1    Ferrer, J.L.2    Bowman, M.E.3    Dixon, R.A.4    Noel, J.P.5
  • 23
    • 0032535449 scopus 로고    scopus 로고
    • A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion
    • Li J, Nishizawa K, An W, Hussey RE, Lialios FE, et al. (1998) A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion. EMBO J 17: 7320-7336.
    • (1998) EMBO J , vol.17 , pp. 7320-7336
    • Li, J.1    Nishizawa, K.2    An, W.3    Hussey, R.E.4    Lialios, F.E.5
  • 24
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18: 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 26
    • 54249122300 scopus 로고    scopus 로고
    • The PCH Family Member Proline-Serine-Threonine Phosphatase-interacting Protein 1 Targets to the Leukocyte Uropod and Regulates Directed Cell Migration
    • Cooper KM, Bennin DA, Huttenlocher A (2008) The PCH Family Member Proline-Serine-Threonine Phosphatase-interacting Protein 1 Targets to the Leukocyte Uropod and Regulates Directed Cell Migration. Mol Biol Cell 19: 3180-3191.
    • (2008) Mol Biol Cell , vol.19 , pp. 3180-3191
    • Cooper, K.M.1    Bennin, D.A.2    Huttenlocher, A.3
  • 27
    • 0030872948 scopus 로고    scopus 로고
    • PSTPIP: A tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase
    • Spencer S, Dowbenko D, Cheng J, Li W, Brush J, et al. (1997) PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase. J Cell Biol 138: 845-860.
    • (1997) J Cell Biol , vol.138 , pp. 845-860
    • Spencer, S.1    Dowbenko, D.2    Cheng, J.3    Li, W.4    Brush, J.5
  • 28
    • 8444230096 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced expression of multiple alternatively spliced MEFV transcripts in human synovial fibroblasts: A prominent splice isoform lacks the C-terminal domain that is highly mutated in familial Mediterranean fever
    • Diaz A, Hu C, Kastner DL, Schaner P, Reginato AM, et al. (2004) Lipopolysaccharide-induced expression of multiple alternatively spliced MEFV transcripts in human synovial fibroblasts: a prominent splice isoform lacks the C-terminal domain that is highly mutated in familial Mediterranean fever. Arthritis Rheum 50: 3679-3689.
    • (2004) Arthritis Rheum , vol.50 , pp. 3679-3689
    • Diaz, A.1    Hu, C.2    Kastner, D.L.3    Schaner, P.4    Reginato, A.M.5
  • 29
    • 57649096298 scopus 로고    scopus 로고
    • The membrane-tubulating potential of amphiphysin 2/BIN1 is dependent on the microtubule-binding cytoplasmic linker protein 170 (CLIP-170)
    • Meunier B, Quaranta M, Daviet L, Hatzoglou A, Leprince C (2009) The membrane-tubulating potential of amphiphysin 2/BIN1 is dependent on the microtubule-binding cytoplasmic linker protein 170 (CLIP-170). Eur J Cell Biol 88: 91-102.
    • (2009) Eur J Cell Biol , vol.88 , pp. 91-102
    • Meunier, B.1    Quaranta, M.2    Daviet, L.3    Hatzoglou, A.4    Leprince, C.5
  • 30
    • 33748288113 scopus 로고    scopus 로고
    • BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature
    • Itoh T, De Camilli P (2006) BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature. Biochim Biophys Acta 1761: 897-912.
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 897-912
    • Itoh, T.1    De Camilli, P.2
  • 31
    • 34447276909 scopus 로고    scopus 로고
    • F-BAR proteins join the BAR family fold
    • Frost A, De Camilli P, Unger VM (2007) F-BAR proteins join the BAR family fold. Structure 15: 751-753.
    • (2007) Structure , vol.15 , pp. 751-753
    • Frost, A.1    De Camilli, P.2    Unger, V.M.3
  • 32
    • 0035914452 scopus 로고    scopus 로고
    • Interaction between pyrin and the apoptotic speck protein (ASC) modulates ASC-induced apoptosis
    • Richards N, Schaner P, Diaz A, Stuckey J, Shelden E, et al. (2001) Interaction between pyrin and the apoptotic speck protein (ASC) modulates ASC-induced apoptosis. J Biol Chem 276: 39320-39329.
    • (2001) J Biol Chem , vol.276 , pp. 39320-39329
    • Richards, N.1    Schaner, P.2    Diaz, A.3    Stuckey, J.4    Shelden, E.5
  • 33
    • 34548031870 scopus 로고    scopus 로고
    • The pyroptosome: A supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation
    • Fernandes-Alnemri T, Wu J, Yu JW, Datta P, Miller B, et al. (2007) The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation. Cell Death Differ 14: 1590-1604.
    • (2007) Cell Death Differ , vol.14 , pp. 1590-1604
    • Fernandes-Alnemri, T.1    Wu, J.2    Yu, J.W.3    Datta, P.4    Miller, B.5
  • 35
    • 40049086567 scopus 로고    scopus 로고
    • Structural basis of membrane invagination by F-BAR domains
    • Frost A, Perera R, Roux A, Spasov K, Destaing O, et al. (2008) Structural basis of membrane invagination by F-BAR domains. Cell 132: 807-817.
    • (2008) Cell , vol.132 , pp. 807-817
    • Frost, A.1    Perera, R.2    Roux, A.3    Spasov, K.4    Destaing, O.5
  • 36
    • 33845315084 scopus 로고    scopus 로고
    • Powering membrane traffic in endocytosis and recycling
    • Soldati T, Schliwa M (2006) Powering membrane traffic in endocytosis and recycling. Nat Rev Mol Cell Biol 7: 897-908.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 897-908
    • Soldati, T.1    Schliwa, M.2
  • 37
    • 4344619558 scopus 로고    scopus 로고
    • The syndapin protein family: Linking membrane trafficking with the cytoskeleton
    • Kessels MM, Qualmann B (2004) The syndapin protein family: linking membrane trafficking with the cytoskeleton. J Cell Sci 117: 3077-3086.
    • (2004) J Cell Sci , vol.117 , pp. 3077-3086
    • Kessels, M.M.1    Qualmann, B.2


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