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Volumn 137, Issue 2, 1997, Pages 305-317

Assembly and intracellular targeting of the βγ subunits of heterotrimeric G proteins

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; MONOCLONAL ANTIBODY;

EID: 0030890789     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.137.2.305     Document Type: Article
Times cited : (28)

References (70)
  • 1
    • 0027639941 scopus 로고
    • Plasmalemmal caveolae and GPI-anchored membrane proteins
    • Anderson, R.G.W. 1993. Plasmalemmal caveolae and GPI-anchored membrane proteins. Curr. Opin. Cell Biol. 5:647-652.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 647-652
    • Anderson, R.G.W.1
  • 2
    • 0018154865 scopus 로고
    • Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens
    • Barnstable, C.J., W.F. Bodmer, G. Brown, G. Galfre, C. Milstein, A.F. Williams, and A. Ziegler. 1978. Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens. Cell. 14:9-20.
    • (1978) Cell , vol.14 , pp. 9-20
    • Barnstable, C.J.1    Bodmer, W.F.2    Brown, G.3    Galfre, G.4    Milstein, C.5    Williams, A.F.6    Ziegler, A.7
  • 3
    • 0023130106 scopus 로고
    • The presence of free G protein β/γ subunits in human neutrophils results in suppression of adenylate cyclase activity
    • Bokoch, G.M. 1987. The presence of free G protein β/γ subunits in human neutrophils results in suppression of adenylate cyclase activity. J. Biol. Chem. 262:589-594.
    • (1987) J. Biol. Chem. , vol.262 , pp. 589-594
    • Bokoch, G.M.1
  • 5
    • 0027055668 scopus 로고
    • Role of heterotrimeric G proteins in membrane traffic
    • Bomsel, M., and K. Mostov. 1992. Role of heterotrimeric G proteins in membrane traffic. Mol. Biol. Cell. 3:1317-1328.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1317-1328
    • Bomsel, M.1    Mostov, K.2
  • 6
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in TX-114 solution
    • Bordier, C. 1981. Phase separation of integral membrane proteins in TX-114 solution. J. Biol. Chem. 256:1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 8
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H.R., D.A. Sanders, and F. Mc Cormick. 1991. The GTPase superfamily: conserved structure and molecular mechanism. Nature (Lond.). 349:117-127.
    • (1991) Nature (Lond.) , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    Mc Cormick, F.3
  • 9
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D.A., and J.K. Rose. 1992. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell. 68:533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 10
    • 0028351930 scopus 로고
    • Lipid modifications of G proteins
    • Casey, P.J. 1994. Lipid modifications of G proteins. Curr. Opin. Cell Biol. 6: 219-225.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 219-225
    • Casey, P.J.1
  • 11
    • 0026625261 scopus 로고
    • Lowering the cholesterol content of MA 104 cells inhibits receptor mediated transport of folate
    • Chang, W.-J., K.G. Rothberg, B.A. Kamen, and R.G.W. Anderson. 1992. Lowering the cholesterol content of MA 104 cells inhibits receptor mediated transport of folate. J. Cell Biol. 118:63-69.
    • (1992) J. Cell Biol. , vol.118 , pp. 63-69
    • Chang, W.-J.1    Rothberg, K.G.2    Kamen, B.A.3    Anderson, R.G.W.4
  • 13
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clarke, S. 1992. Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Annu. Rev. Biochem. 61:355-386.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 355-386
    • Clarke, S.1
  • 14
    • 0018820017 scopus 로고
    • Potential mechanism of insulin action on glucose transport in the isolated rat adipose cell
    • Cushman, S.W., and L.J. Wardzala. 1980. Potential mechanism of insulin action on glucose transport in the isolated rat adipose cell. J. Biol. Chem. 255:4758-4762.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4758-4762
    • Cushman, S.W.1    Wardzala, L.J.2
  • 15
    • 0029929903 scopus 로고    scopus 로고
    • Differential distribution of α subunits and βγ subunits of heterotrimeric G proteins on Golgi membranes of the exocrine pancreas
    • Denker, S.P., J.M. Mc Caffery, G.E. Palade, P.A. Insel, and M.G. Farquhar. 1996. Differential distribution of α subunits and βγ subunits of heterotrimeric G proteins on Golgi membranes of the exocrine pancreas. J. Cell Biol. 133:1027-1040.
    • (1996) J. Cell Biol. , vol.133 , pp. 1027-1040
    • Denker, S.P.1    Mc Caffery, J.M.2    Palade, G.E.3    Insel, P.A.4    Farquhar, M.G.5
  • 16
    • 0020975121 scopus 로고
    • Characterization of transducin from bovine retinal rod outer segments
    • Fung, B.K.-K., and C.R. Nash. 1983. Characterization of transducin from bovine retinal rod outer segments. J. Biol. Chem. 258:10503-10510.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10503-10510
    • Fung, B.K.-K.1    Nash, C.R.2
  • 17
    • 0029142888 scopus 로고
    • Inhibition of sphingolipid synthesis: Effects on glycosphingolipid-GPI-anchored protein microdomains
    • Futerman, A.H. 1995. Inhibition of sphingolipid synthesis: effects on glycosphingolipid-GPI-anchored protein microdomains. Trends Cell Biol. 5: 377-380.
    • (1995) Trends Cell Biol. , vol.5 , pp. 377-380
    • Futerman, A.H.1
  • 18
    • 0030039493 scopus 로고    scopus 로고
    • Intersubunit surfaces in G protein αβγ heterotrimers
    • Garcia-Higuera, I., T.C. Thomas. F. Yi, and E.J. Neer. 1996. Intersubunit surfaces in G protein αβγ heterotrimers. J. Biol. Chem. 271:528-535.
    • (1996) J. Biol. Chem. , vol.271 , pp. 528-535
    • Garcia-Higuera, I.1    Thomas, T.C.2    Yi, F.3    Neer, E.J.4
  • 19
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman, A.G. 1987. G proteins: transducers of receptor-generated signals. Anim. Rev. Biochem. 56:615-649.
    • (1987) Anim. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 20
    • 0028926204 scopus 로고
    • Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin
    • Gorodinsky, A., and D.A. Harris. 1995. Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin. J. Cell Biol. 129:619-627.
    • (1995) J. Cell Biol. , vol.129 , pp. 619-627
    • Gorodinsky, A.1    Harris, D.A.2
  • 21
    • 0023580391 scopus 로고
    • Kinetics of intracellular transport and sorting of lysosomal membrane and plasma membrane proteins
    • Green, S.A., K.-P. Zimmer, G. Griffiths, and I. Mellman. 1987. Kinetics of intracellular transport and sorting of lysosomal membrane and plasma membrane proteins. J. Cell Biol. 105:1227-1240.
    • (1987) J. Cell Biol. , vol.105 , pp. 1227-1240
    • Green, S.A.1    Zimmer, K.-P.2    Griffiths, G.3    Mellman, I.4
  • 22
    • 0024465343 scopus 로고
    • Posttranslational processing of p21 ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis
    • Gutierrez, L., A.I. Magee, C.J. Marshall, and J.F. Hancock. 1989. Posttranslational processing of p21 ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis. EMBO (Eur. Mol. Biol. Organ.) J. 8:1093-1098.
    • (1989) EMBO (Eur. Mol. Biol. Organ.) J. , vol.8 , pp. 1093-1098
    • Gutierrez, L.1    Magee, A.I.2    Marshall, C.J.3    Hancock, J.F.4
  • 23
    • 0026021456 scopus 로고
    • Methylation and proteolysis are essential for efficient membrane binding of prenylated p21 k-ras (B)
    • Hancock, J.F., K. Cadwallader, and C.J. Marshall. 1991. Methylation and proteolysis are essential for efficient membrane binding of prenylated p21 k-ras (B). EMBO (Eur. Mol. Biol. Organ.) J. 10:641-646.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 641-646
    • Hancock, J.F.1    Cadwallader, K.2    Marshall, C.J.3
  • 24
    • 0026803223 scopus 로고
    • G protein-coupled mechanisms and nervous signaling
    • Hille, B. 1992. G protein-coupled mechanisms and nervous signaling. Neuron. 9:187-195.
    • (1992) Neuron , vol.9 , pp. 187-195
    • Hille, B.1
  • 26
    • 0025101546 scopus 로고
    • Myristoylation of an inhibitory GTP-binding protein α subunit is essential for its membrane attachment
    • Jones, T.L.Z., W.F. Simonds, J.J. Merendino, M.R. Brann, and A.M. Spiegel. 1990. Myristoylation of an inhibitory GTP-binding protein α subunit is essential for its membrane attachment. Proc. Natl. Acad. Sci. USA. 87: 568-572.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 568-572
    • Jones, T.L.Z.1    Simonds, W.F.2    Merendino, J.J.3    Brann, M.R.4    Spiegel, A.M.5
  • 27
    • 0026764981 scopus 로고
    • sα are localized to the particulate fraction of transfected COS cells
    • sα are localized to the particulate fraction of transfected COS cells. J. Cell Biol. 119:523-530.
    • (1992) J. Cell Biol. , vol.119 , pp. 523-530
    • Juhnn, Y.-S.1    Jones, T.L.Z.2    Spiegel, A.M.3
  • 28
    • 0026561901 scopus 로고
    • Brefeldin A: Insight into the control of membrane traffic and organelle structure
    • Klausner, R.D., J.G. Donaklson, and J. Lippincott-Schwartz. 1992. Brefeldin A: insight into the control of membrane traffic and organelle structure. J. Cell Biol. 116:1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaklson, J.G.2    Lippincott-Schwartz, J.3
  • 29
    • 0026752495 scopus 로고
    • Different β-subunits determine G-protein interaction with transmembrane receptors
    • Kleuss, C., H. Scheruebl, J. Hescheler, G. Schultz, and B. Wittig. 1992. Different β-subunits determine G-protein interaction with transmembrane receptors. Nature (Lond.). 358:424-426.
    • (1992) Nature (Lond.) , vol.358 , pp. 424-426
    • Kleuss, C.1    Scheruebl, H.2    Hescheler, J.3    Schultz, G.4    Wittig, B.5
  • 30
    • 0030474342 scopus 로고    scopus 로고
    • Identification of Triton X-100 insoluble domains in the yeast Saccharomyces cerevisiae
    • Kuebler, E., H.G. Dohlman, and M.P. Lisanti. 1996. Identification of Triton X-100 insoluble domains in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 271:32975-32980.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32975-32980
    • Kuebler, E.1    Dohlman, H.G.2    Lisanti, M.P.3
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0028896344 scopus 로고
    • Activation of Tsk and Btk tyrosine kinases by G protein βγ subunits
    • Langhans-Rajasekaran, S., Y. Wan, and X.-Y. Huang. 1995. Activation of Tsk and Btk tyrosine kinases by G protein βγ subunits. Proc. Natl. Acad. Sci. USA. 92:8601-8605.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8601-8605
    • Langhans-Rajasekaran, S.1    Wan, Y.2    Huang, X.-Y.3
  • 33
    • 0026474549 scopus 로고
    • Activation of the α subunit of Gs in intact cells alters its abundance, rate of degradation, and membrane avidity
    • Levis, M.J., and H.R. Bourne. 1992. Activation of the α subunit of Gs in intact cells alters its abundance, rate of degradation, and membrane avidity. J. Cell Biol. 119:1297-1307.
    • (1992) J. Cell Biol. , vol.119 , pp. 1297-1307
    • Levis, M.J.1    Bourne, H.R.2
  • 35
    • 0000441994 scopus 로고
    • Polarized apical distribution of glycosyl-phosphatidylinositol-anchored proteins in a renal epithelial cell line
    • Lisanti, M.P., M. Sargiacomo, L Graeve, A.R. Saltiel, and E. Rodriguez-Boulan. 1988. Polarized apical distribution of glycosyl-phosphatidylinositol-anchored proteins in a renal epithelial cell line. Proc. Natl. Acad. Sci. USA. 85:9557-9561.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9557-9561
    • Lisanti, M.P.1    Sargiacomo, M.2    Graeve, L.3    Saltiel, A.R.4    Rodriguez-Boulan, E.5
  • 36
    • 0028285191 scopus 로고
    • Caveolae, caveolin and caveolin-rich membrane domains: A signalling hypothesis
    • Lisanti, M.P., P.E. Scherer, and Z.L. Tang. 1994. Caveolae, caveolin and caveolin-rich membrane domains: a signalling hypothesis. Trends Cell Biol. 4:231-235.
    • (1994) Trends Cell Biol. , vol.4 , pp. 231-235
    • Lisanti, M.P.1    Scherer, P.E.2    Tang, Z.L.3
  • 37
    • 0027363575 scopus 로고
    • Caveolin forms a hetero-oligomeric protein complex that interacts with an apical GPI-linked protein: Implications for the biogenesis of caveolae
    • Lisanti, M.P., Z.L. Tang, and M. Sargiacomo. 1993. Caveolin forms a hetero-oligomeric protein complex that interacts with an apical GPI-linked protein: implications for the biogenesis of caveolae. J. Cell Biol. 123:595-604.
    • (1993) J. Cell Biol. , vol.123 , pp. 595-604
    • Lisanti, M.P.1    Tang, Z.L.2    Sargiacomo, M.3
  • 39
    • 0027284950 scopus 로고
    • Protein prenylation: A mediator of protein-protein interactions
    • Marshall, C.J. 1993. Protein prenylation: a mediator of protein-protein interactions. Science (Wash. DC). 259:1865-1866.
    • (1993) Science (Wash. DC) , vol.259 , pp. 1865-1866
    • Marshall, C.J.1
  • 40
    • 0029166488 scopus 로고
    • Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells
    • Mays, R.W., K.A. Siemers, B.A. Fritz, A.W. Lowe, G. van Meer, and W.J. Nelson. 1995. Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells. J. Cell Biol. 130:1105-1115.
    • (1995) J. Cell Biol. , vol.130 , pp. 1105-1115
    • Mays, R.W.1    Siemers, K.A.2    Fritz, B.A.3    Lowe, A.W.4    Van Meer, G.5    Nelson, W.J.6
  • 41
    • 0029039937 scopus 로고
    • The dynamic role of palmitoylation in signal transduction
    • Milligan, G., M. Parenti, and A.I. Magee. 1995. The dynamic role of palmitoylation in signal transduction. TIBS. 20:181-186.
    • (1995) TIBS , vol.20 , pp. 181-186
    • Milligan, G.1    Parenti, M.2    Magee, A.I.3
  • 43
    • 2142858516 scopus 로고
    • Antisera of designed specificity for subunits of guanine nucleotide-binding regulatory proteins
    • Mumby, S.M., R.A. Kahn, D.R. Manning, and A.G. Gilman. 1986. Antisera of designed specificity for subunits of guanine nucleotide-binding regulatory proteins. Proc. Natl. Acad Sci. USA. 83:265-269.
    • (1986) Proc. Natl. Acad Sci. USA , vol.83 , pp. 265-269
    • Mumby, S.M.1    Kahn, R.A.2    Manning, D.R.3    Gilman, A.G.4
  • 44
    • 0025012836 scopus 로고
    • G-protein α-subunit expression, myristoylation, and membrane association in COS cells
    • Mumby, S.M., R.O. Heukeroth, J.I. Gordon, and A.G. Gilman. 1990. G-protein α-subunit expression, myristoylation, and membrane association in COS cells. Proc. Natl. Acad. Sci. USA. 87:728-732.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 728-732
    • Mumby, S.M.1    Heukeroth, R.O.2    Gordon, J.I.3    Gilman, A.G.4
  • 45
    • 0027090202 scopus 로고
    • Influence of γ subunit prenylation on association of guanine nucleotide-binding regulatory proteins with membranes
    • Muntz, K.H., P.C. Sternweis, A.G. Gilman, and S.M. Mumby. 1992. Influence of γ subunit prenylation on association of guanine nucleotide-binding regulatory proteins with membranes. Mol. Biol. Cell. 3:49-61.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 49-61
    • Muntz, K.H.1    Sternweis, P.C.2    Gilman, A.G.3    Mumby, S.M.4
  • 46
    • 0028860268 scopus 로고
    • Heterotrimeric G proteins: Organizers of transmembrane signals
    • Neer, E.J. 1995. Heterotrimeric G proteins: organizers of transmembrane signals. Cell. 80:249-257.
    • (1995) Cell , vol.80 , pp. 249-257
    • Neer, E.J.1
  • 47
    • 0024284962 scopus 로고
    • Roles of G protein subunits in transmembrane signalling
    • Neer, E.J., and D.E. Clapham. 1988. Roles of G protein subunits in transmembrane signalling. Nature (Lond.). 333:129-134.
    • (1988) Nature (Lond.) , vol.333 , pp. 129-134
    • Neer, E.J.1    Clapham, D.E.2
  • 48
    • 0021244750 scopus 로고
    • Photoaffinity labeling of insulin-sensitive hexose transporters in intact rat adipocytes
    • Oka, Y., and M.P. Czech. 1984. Photoaffinity labeling of insulin-sensitive hexose transporters in intact rat adipocytes. J. Biol. Chem. 259:8125-8133.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8125-8133
    • Oka, Y.1    Czech, M.P.2
  • 49
    • 0020536403 scopus 로고
    • Insulin action rapidly modulates the apparent affinity of the insulin-like growth factor II receptor
    • Oppenheimer, C.L., J.E. Pessin, J. Massague, W. Gitomer, and M.P. Czech. 1983. Insulin action rapidly modulates the apparent affinity of the insulin-like growth factor II receptor. J. Biol. Chem. 258:4824-4830.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4824-4830
    • Oppenheimer, C.L.1    Pessin, J.E.2    Massague, J.3    Gitomer, W.4    Czech, M.P.5
  • 51
    • 0028126950 scopus 로고
    • Differential coupling of G protein α subunits to seven-helix receptors expressed in Xenopus oocytes
    • Quick, M.W., M.I. Simon, N. Davidson, H.A. Lester, and A.M. Aragay. 1994. Differential coupling of G protein α subunits to seven-helix receptors expressed in Xenopus oocytes. J. Biol. Chem. 269:30164-30172.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30164-30172
    • Quick, M.W.1    Simon, M.I.2    Davidson, N.3    Lester, H.A.4    Aragay, A.M.5
  • 52
    • 0031046889 scopus 로고    scopus 로고
    • Monoclonal antibodies that distinguish free and complexed heterotrimeric G protein β subunits
    • Rehm, A., and H.L. Ploegh. 1997. Monoclonal antibodies that distinguish free and complexed heterotrimeric G protein β subunits. FEBS Lett. 402: 277-285.
    • (1997) FEBS Lett. , vol.402 , pp. 277-285
    • Rehm, A.1    Ploegh, H.L.2
  • 53
    • 0024709982 scopus 로고
    • Signal sorting and amplification through G protein-coupled receptors
    • Ross, E.M. 1989. Signal sorting and amplification through G protein-coupled receptors. Neuron. 3:141-152.
    • (1989) Neuron , vol.3 , pp. 141-152
    • Ross, E.M.1
  • 54
    • 0025303751 scopus 로고
    • The glycophospholipid-linked folate receptor internalizes folate without entering the clathrin-coated pit endocytic pathway
    • Rothberg, K.G., Y.S. Ying, J.F. Kolhouse, B.A. Kamen, and R.G.W. Anderson. 1990. The glycophospholipid-linked folate receptor internalizes folate without entering the clathrin-coated pit endocytic pathway. J. Cell Biol. 110:637-649.
    • (1990) J. Cell Biol. , vol.110 , pp. 637-649
    • Rothberg, K.G.1    Ying, Y.S.2    Kolhouse, J.F.3    Kamen, B.A.4    Anderson, R.G.W.5
  • 55
    • 0028175989 scopus 로고
    • Cysteine of src family kinases determines palmitoylation and localization in caveolae
    • Shenoy-Scaria, A.M., D.J. Dietzen, J. Kwong, D.C. Link, and D.M. Lublin. 1994. Cysteine of src family kinases determines palmitoylation and localization in caveolae. J. Cell Biol. 126:353-363.
    • (1994) J. Cell Biol. , vol.126 , pp. 353-363
    • Shenoy-Scaria, A.M.1    Dietzen, D.J.2    Kwong, J.3    Link, D.C.4    Lublin, D.M.5
  • 56
  • 57
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons, K., and G. van Meer. 1988. Lipid sorting in epithelial cells. Biochemistry. 27:6197-6202.
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 58
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons, K., and A. Wandinger-Ness. 1990. Polarized sorting in epithelia. Cell. 62:207-210.
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 59
    • 0024547523 scopus 로고
    • Differential extractibility of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts
    • Skibbens, J.E., M.G. Roth, and K.S. Matlin. 1989. Differential extractibility of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts. J. Cell Biol. 108:821-832.
    • (1989) J. Cell Biol. , vol.108 , pp. 821-832
    • Skibbens, J.E.1    Roth, M.G.2    Matlin, K.S.3
  • 60
    • 0027952583 scopus 로고
    • Protein kinase C activators inhibit receptor-mediated potocytosis by preventing internalization of caveolae
    • Smart, E.J., D.C. Foster, Y.S. Ying, B.A. Kamen, and R.G.W. Anderson. 1994. Protein kinase C activators inhibit receptor-mediated potocytosis by preventing internalization of caveolae. J. Cell Biol. 124:307-314.
    • (1994) J. Cell Biol. , vol.124 , pp. 307-314
    • Smart, E.J.1    Foster, D.C.2    Ying, Y.S.3    Kamen, B.A.4    Anderson, R.G.W.5
  • 61
    • 0028125208 scopus 로고
    • Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation
    • Smart, J.E., Y.S. Ying, P.A. Conrad, and R.G.W. Anderson. 1994. Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation. J. Cell Biol. 127:1185-1197.
    • (1994) J. Cell Biol. , vol.127 , pp. 1185-1197
    • Smart, J.E.1    Ying, Y.S.2    Conrad, P.A.3    Anderson, R.G.W.4
  • 62
    • 0029912981 scopus 로고    scopus 로고
    • Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains
    • Song, K.S., S. Li, T. Okamoto, L.A. Quilliam, M. Sargiacomo, and M.P. Lisanti. 1996. Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. J. Biol. Chem. 271:9690-9697.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9690-9697
    • Song, K.S.1    Li, S.2    Okamoto, T.3    Quilliam, L.A.4    Sargiacomo, M.5    Lisanti, M.P.6
  • 63
    • 0022608859 scopus 로고
    • i from bovine brain require βγ for association with phospholipid vesicles
    • i from bovine brain require βγ for association with phospholipid vesicles. J. Biol. Chem. 261:631-637.
    • (1986) J. Biol. Chem. , vol.261 , pp. 631-637
    • Sternweis, P.C.1
  • 64
    • 0027295485 scopus 로고
    • G protein βγ subunit: Physical and chemical characterisation
    • Thomas, C.T., T. Sladek, F. Yi, T. Smith, and E.J. Neer. 1993. G protein βγ subunit: physical and chemical characterisation. Biochemistry. 32:8628-8635.
    • (1993) Biochemistry , vol.32 , pp. 8628-8635
    • Thomas, C.T.1    Sladek, T.2    Yi, F.3    Smith, T.4    Neer, E.J.5
  • 65
    • 0028352175 scopus 로고
    • Large-scale co-aggregation of fluorescent lipid probes with cell surface proteins
    • Thomas, J.L., D. Holowka, B. Baird, and W.W. Webb. 1994. Large-scale co-aggregation of fluorescent lipid probes with cell surface proteins. J. Cell Biol. 125:795-802.
    • (1994) J. Cell Biol. , vol.125 , pp. 795-802
    • Thomas, J.L.1    Holowka, D.2    Baird, B.3    Webb, W.W.4
  • 66
    • 0028173394 scopus 로고
    • Binding of βγ subunits of heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase
    • Tsukada, S., M.I. Simon, O.N. Witte, and A. Katz. 1994. Binding of βγ subunits of heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase. Proc. Natl. Acad. Sci. USA. 91:11256-11260.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11256-11260
    • Tsukada, S.1    Simon, M.I.2    Witte, O.N.3    Katz, A.4
  • 68
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US 11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • Wiertz, E.J.H.J., T.R. Jones, L. Sun, M. Bogyo, H.J. Geuze, and H.L. Ploegh. 1996. The human cytomegalovirus US 11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell. 84:769-779.
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.H.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 70
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F.L., and P.J. Casey. 1996. Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65:241-269.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2


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