메뉴 건너뛰기




Volumn 585, Issue 21, 2011, Pages 3485-3490

Ca2+-calmodulin inhibits tail-anchored protein insertion into the mammalian endoplasmic reticulum membrane

Author keywords

Calcium; Calmodulin; Membrane insertion; Tail anchored membrane proteins; Trifluoperazine

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; CALCIUM ION; CYTOCHROME B5; MEMBRANE PROTEIN; SYNAPTOBREVIN 2; TRIFLUOPERAZINE; CALCIUM; CALMODULIN;

EID: 80255129394     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.10.008     Document Type: Article
Times cited : (21)

References (34)
  • 2
    • 33947202862 scopus 로고    scopus 로고
    • The tail end of membrane insertion
    • E. Mandon, and R. Gilmore The tail end of membrane insertion Cell 128 2007 1031 1332
    • (2007) Cell , vol.128 , pp. 1031-1332
    • Mandon, E.1    Gilmore, R.2
  • 3
    • 79851511792 scopus 로고    scopus 로고
    • Targeting pathways of C-tail-anchored proteins
    • N. Borgese, and E. Fasana Targeting pathways of C-tail-anchored proteins Biochem. Biophys. Acta 1808 2011 937 946
    • (2011) Biochem. Biophys. Acta , vol.1808 , pp. 937-946
    • Borgese, N.1    Fasana, E.2
  • 6
    • 3543016171 scopus 로고    scopus 로고
    • Signal recognition particle mediates post-translational targeting in eukaryotes
    • DOI 10.1038/sj.emboj.7600281
    • B.M. Abell, M.R. Pool, O. Schlenker, I. Sinning, and S. High Signal recognition particle mediates post-translational targeting in eukaryotes EMBO J. 23 2004 2755 2764 (Pubitemid 39013548)
    • (2004) EMBO Journal , vol.23 , Issue.14 , pp. 2755-2764
    • Abell, B.M.1    Pool, M.R.2    Schlenker, O.3    Sinning, I.4    High, S.5
  • 7
    • 34250183921 scopus 로고    scopus 로고
    • Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones
    • DOI 10.1242/jcs.002410
    • B.M. Abell, C. Rabu, P. Leznicki, J.C. Young, and S. High Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones J. Cell Sci. 120 2007 1743 1751 (Pubitemid 46930412)
    • (2007) Journal of Cell Science , vol.120 , Issue.10 , pp. 1743-1751
    • Abell, B.M.1    Rabu, C.2    Leznicki, P.3    Young, J.C.4    High, S.5
  • 8
    • 33947218544 scopus 로고    scopus 로고
    • Identification of a Targeting Factor for Posttranslational Membrane Protein Insertion into the ER
    • DOI 10.1016/j.cell.2007.01.036, PII S009286740700195X
    • S. Stefanovic, and R.S. Hegde Identification of a targeting factor for posttranslational membrane protein insertion into the ER Cell 128 2007 1147 1159 (Pubitemid 46427870)
    • (2007) Cell , vol.128 , Issue.6 , pp. 1147-1159
    • Stefanovic, S.1    Hegde, R.S.2
  • 9
    • 46749104133 scopus 로고    scopus 로고
    • Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins
    • DOI 10.1242/jcs.020321
    • V. Favaloro, M. Spasic, B. Schwappach, and B. Dobberstein Distinct targeting pathways fort the membrane insertion of tail-anchored (TA) proteins J. Cell Sci. 121 2008 1832 1840 (Pubitemid 351943376)
    • (2008) Journal of Cell Science , vol.121 , Issue.11 , pp. 1832-1840
    • Favaloro, V.1    Spasic, M.2    Schwappach, B.3    Dobberstein, B.4
  • 10
    • 55549102665 scopus 로고    scopus 로고
    • A precursor-specific role for Hsp40/Hsc70 during tail-anchored protein integration at the endoplasmic reticulum
    • C. Rabu, P. Wipf, J.L. Brodsky, and S. High A precursor-specific role for Hsp40/Hsc70 during tail-anchored protein integration at the endoplasmic reticulum J. Biol. Chem. 283 2008 27504 27513
    • (2008) J. Biol. Chem. , vol.283 , pp. 27504-27513
    • Rabu, C.1    Wipf, P.2    Brodsky, J.L.3    High, S.4
  • 11
    • 70350359860 scopus 로고    scopus 로고
    • Biogenesis of tail-anchored proteins: The beginning for the end?
    • C. Rabu, V. Schmid, B. Schwappach, and S. High Biogenesis of tail-anchored proteins: the beginning for the end? J. Cell Sci. 122 2009 3605 3612
    • (2009) J. Cell Sci. , vol.122 , pp. 3605-3612
    • Rabu, C.1    Schmid, V.2    Schwappach, B.3    High, S.4
  • 12
    • 77954352789 scopus 로고    scopus 로고
    • Bat3 promotes the membrane integration of tail-anchored proteins
    • P. Leznicki, A. Clancy, B. Schwappach, and S. High Bat3 promotes the membrane integration of tail-anchored proteins. J. Cell Sci. 123 2010 2170 2178
    • (2010) J. Cell Sci. , vol.123 , pp. 2170-2178
    • Leznicki, P.1    Clancy, A.2    Schwappach, B.3    High, S.4
  • 15
    • 23044492259 scopus 로고    scopus 로고
    • Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition
    • DOI 10.1038/sj.emboj.7600730
    • S. Brambillasca, M. Yabal, P. Soffientini, S. Stefanovic, M. Makarow, R.S. Hegde, and N. Borgese Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition EMBO J. 24 2005 2533 2542 (Pubitemid 41076310)
    • (2005) EMBO Journal , vol.24 , Issue.14 , pp. 2533-2542
    • Brambillasca, S.1    Yabal, M.2    Soffientini, P.3    Stefanovic, S.4    Makarow, M.5    Hegde, R.S.6    Borgese, N.7
  • 16
    • 33845307248 scopus 로고    scopus 로고
    • Unassisted translocation of large polypeptide domains across phospholipid bilayers
    • DOI 10.1083/jcb.200608101
    • S. Brambillasca, M. Yabal, M. Makarow, and N. Borgese Unassisted translocation of large polypeptide domains across phospholipid bilayers J. Cell Biol. 175 2006 767 777 (Pubitemid 44878509)
    • (2006) Journal of Cell Biology , vol.175 , Issue.5 , pp. 767-777
    • Brambillasca, S.1    Yabal, M.2    Makarow, M.3    Borgese, N.4
  • 17
    • 69649091942 scopus 로고    scopus 로고
    • The role of cytosolic proteins in the insertion of tail-anchored proteins into phospholipid bilayers
    • S.F. Colombo, R. Longhi, and N. Borgese The role of cytosolic proteins in the insertion of tail-anchored proteins into phospholipid bilayers J. Cell Sci. 122 2009 2383 2392
    • (2009) J. Cell Sci. , vol.122 , pp. 2383-2392
    • Colombo, S.F.1    Longhi, R.2    Borgese, N.3
  • 18
    • 79953137111 scopus 로고    scopus 로고
    • WRB is the recpetor for TRC40/Asna-1-mediated insertion of tail-anchored proteins into the ER membrane
    • F. Vilardi, H. Lorenz, and B. Dobberstein WRB is the recpetor for TRC40/Asna-1-mediated insertion of tail-anchored proteins into the ER membrane J. Cell Sci. 124 2011 1301 1307
    • (2011) J. Cell Sci. , vol.124 , pp. 1301-1307
    • Vilardi, F.1    Lorenz, H.2    Dobberstein, B.3
  • 19
    • 0028837490 scopus 로고
    • Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane
    • U. Kutay, G. Ahnert-Hilger, E. Hartmann, B. Wiedenmann, and T.A. Rapoport Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane EMBO J. 14 1995 217 223
    • (1995) EMBO J. , vol.14 , pp. 217-223
    • Kutay, U.1    Ahnert-Hilger, G.2    Hartmann, E.3    Wiedenmann, B.4    Rapoport, T.A.5
  • 20
    • 0025740247 scopus 로고
    • A microsomal protein is involved in ATP-dependent transport of presecretory proteins into mammalian microsomes
    • P. Klappa, P. Mayinger, R. Pipkorn, M. Zimmermann, and R. Zimmermann A microsomal protein is involved in ATP-dependent transport of presecretory proteins into mammalian microsomes EMBO J. 10 1991 2795 2803 (Pubitemid 21905296)
    • (1991) EMBO Journal , vol.10 , Issue.10 , pp. 2795-2803
    • Klappa, P.1    Mayinger, P.2    Pipkorn, R.3    Zimmermann, M.4    Zimmermann, R.5
  • 21
    • 0029024163 scopus 로고
    • The translocation, folding, assembly, and redox-dependent degradation of secretory an membrane proteins in semi-permeabilized mammalian cells
    • R. Wilson, A.J. Allen, J. Oliver, J.L. Brookman, S. High, and N.J. Bulleid The translocation, folding, assembly, and redox-dependent degradation of secretory an membrane proteins in semi-permeabilized mammalian cells Biochem. J. 387 1995 679 687
    • (1995) Biochem. J. , vol.387 , pp. 679-687
    • Wilson, R.1    Allen, A.J.2    Oliver, J.3    Brookman, J.L.4    High, S.5    Bulleid, N.J.6
  • 22
    • 0023680171 scopus 로고
    • The sites on calmodulin cross-linked to myosin light chain kinase and troponin i with water-soluble carbodiimide
    • K. Yamamoto, T. Sekine, and K. Sutoh The sites on calmodulin cross-linked to myosin light chain kinase and troponin I with water-soluble carbodiimide J. Biochem. 104 1988 251 254
    • (1988) J. Biochem. , vol.104 , pp. 251-254
    • Yamamoto, K.1    Sekine, T.2    Sutoh, K.3
  • 23
    • 0027214861 scopus 로고
    • The calmodulin-binding domain of the mouse 90-kDa heat shock protein
    • Y. Minami, H. Kawasaki, K. Suzuki, and I. Yahara The calmodulin-binding domain of the mouse 90-kDa heat shock protein J. Biol. Chem. 268 1993 9604 9610 (Pubitemid 23146018)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.13 , pp. 9604-9610
    • Minami, Y.1    Kawasaki, H.2    Suzuki, K.3    Yahara, I.4
  • 26
    • 0002708827 scopus 로고    scopus 로고
    • Calmodulin
    • M.R. Celio, T.L. Pauls, B. Schwaller, Oxford University Press Oxford, UK
    • M.S. Rogers, and E.E. Strehler Calmodulin M.R. Celio, T.L. Pauls, B. Schwaller, Guidebook to the Calcium-binding Proteins 1996 Oxford University Press Oxford, UK 34 40
    • (1996) Guidebook to the Calcium-binding Proteins , pp. 34-40
    • Rogers, M.S.1    Strehler, E.E.2
  • 30
    • 0036683087 scopus 로고    scopus 로고
    • Calmodulin and lipid binding to synaptobrevin regulates calcium-dependent exocytosis
    • DOI 10.1093/emboj/cdf404
    • S. Quetglas, C. Iborra, N. Sasakawa, L. De Haro, C. Kumakura, K. Sato, C. Leveque, and M. Seagar Calmodulin and lipid binding to synaptobrevin regulates calcium-dependent exocytosis EMBO J. 21 2002 3970 3979 (Pubitemid 34857430)
    • (2002) EMBO Journal , vol.21 , Issue.15 , pp. 3970-3979
    • Quetglas, S.1    Iborra, C.2    Sasakawa, N.3    De Haro, L.4    Kumakura, K.5    Sato, K.6    Leveque, C.7    Seagar, M.8
  • 31
    • 77954928730 scopus 로고    scopus 로고
    • Calcium-dependent regulation of SNARE-mediated membrane fusion by calmodulin
    • J. DiGiovanni, C. Iborra, Y. Maulet, C. Leveque, O. El Far, and M. Seagar Calcium-dependent regulation of SNARE-mediated membrane fusion by calmodulin J. Biol. Chem. 285 2010 23665 23675
    • (2010) J. Biol. Chem. , vol.285 , pp. 23665-23675
    • Digiovanni, J.1    Iborra, C.2    Maulet, Y.3    Leveque, C.4    El Far, O.5    Seagar, M.6
  • 33
    • 47649126755 scopus 로고    scopus 로고
    • Integration of tail-anchored proteins into the mitochondrial outer membrane does not require any known import components
    • DOI 10.1242/jcs.024034
    • C. Kemper, S.J. Habib, G. Engl, P. Heckmeyer, K.S. Dimmer, and D. Rapaport Integration of tail-anchored proteins into the mitochondrial outer membrane does not require any known import components J. Cell Sci. 121 2008 1990 1998 (Pubitemid 352015196)
    • (2008) Journal of Cell Science , vol.121 , Issue.12 , pp. 1990-1998
    • Kemper, C.1    Habib, S.J.2    Engl, G.3    Heckmeyer, P.4    Dimmer, K.S.5    Rapaport, D.6
  • 34
    • 77957376226 scopus 로고    scopus 로고
    • A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum
    • F. Wang, E.C. Brown, G. Mak, J. Zhuang, and V. Denic A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum Mol. Cell 40 2010 1 13
    • (2010) Mol. Cell , vol.40 , pp. 1-13
    • Wang, F.1    Brown, E.C.2    Mak, G.3    Zhuang, J.4    Denic, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.