메뉴 건너뛰기




Volumn 210, Issue 2, 1998, Pages 229-237

Identification, sequence and developmental expression of invertebrate flotillins from Drosophila melanogaster

Author keywords

Caveolae; Caveolins; Flotillin gene family; Signal transduction

Indexed keywords

CAVEOLIN; COMPLEMENTARY DNA; FLOTILLIN; MEMBRANE ANTIGEN; MEMBRANE PROTEIN; MESSENGER RNA; UNCLASSIFIED DRUG;

EID: 0032515945     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00064-X     Document Type: Article
Times cited : (54)

References (47)
  • 1
    • 0003455530 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • Ashburner, M., 1989. Drosophila, a Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989) Drosophila, a Laboratory Manual
    • Ashburner, M.1
  • 2
    • 0031010267 scopus 로고    scopus 로고
    • Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins
    • Bickel P.E., Scherer P.E., Schnitzer J., Oh P., Lisanti M.P., Lodish H.F. Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins. J. Biol. Chem. 272:1997;13793-13802.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13793-13802
    • Bickel, P.E.1    Scherer, P.E.2    Schnitzer, J.3    Oh, P.4    Lisanti, M.P.5    Lodish, H.F.6
  • 3
    • 0017623256 scopus 로고
    • Membrane-associated vesicles in fibroblasts
    • Bretscher M., Whytock S. Membrane-associated vesicles in fibroblasts. J. Ultrastruct. Res. 61:1977;215-217.
    • (1977) J. Ultrastruct. Res. , vol.61 , pp. 215-217
    • Bretscher, M.1    Whytock, S.2
  • 6
    • 0029019438 scopus 로고
    • Insulin stimulates the tyrosine phosphorylation of caveolin
    • Corley-Mastick C., Brady M.J., Saltiel A.R. Insulin stimulates the tyrosine phosphorylation of caveolin. J. Cell Biol. 129:1995;1523-1531.
    • (1995) J. Cell Biol. , vol.129 , pp. 1523-1531
    • Corley-Mastick, C.1    Brady, M.J.2    Saltiel, A.R.3
  • 8
    • 0028920139 scopus 로고
    • Caveolin is palmitoylated on multiple cysteine residues: Palmitoylation is not necessary for localization of caveolin to caveolae
    • Dietzen D.J., Hastings W.R., Lublin D.M. Caveolin is palmitoylated on multiple cysteine residues: palmitoylation is not necessary for localization of caveolin to caveolae. J. Biol. Chem. 270:1995;6838-6842.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6838-6842
    • Dietzen, D.J.1    Hastings, W.R.2    Lublin, D.M.3
  • 9
    • 0020645545 scopus 로고
    • Morphological changes of the 3T3-L1 fibroblast plasma membrane upon differentiation to the adipocyte form
    • Fan J.Y., Carpentier J.-L., van Obberghen E., Grunfeld C., Gorden P., Orci L. Morphological changes of the 3T3-L1 fibroblast plasma membrane upon differentiation to the adipocyte form. J. Cell Sci. 61:1983;219-230.
    • (1983) J. Cell Sci. , vol.61 , pp. 219-230
    • Fan, J.Y.1    Carpentier, J.-L.2    Van Obberghen, E.3    Grunfeld, C.4    Gorden, P.5    Orci, L.6
  • 10
    • 0018584243 scopus 로고
    • Caveolar systems and sarcoplasmic reticulum in coronary smooth muscle cells
    • Forbes M.S., Rennels M., Nelson E. Caveolar systems and sarcoplasmic reticulum in coronary smooth muscle cells. J. Ultrastruct. Res. 67:1979;325-339.
    • (1979) J. Ultrastruct. Res. , vol.67 , pp. 325-339
    • Forbes, M.S.1    Rennels, M.2    Nelson, E.3
  • 11
    • 0029910141 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1
    • Garcia-Cardena G., Fan R., Stern D., Liu J., Sessa W. Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1. J. Biol. Chem. 271:1996;27237-27240.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27237-27240
    • Garcia-Cardena, G.1    Fan, R.2    Stern, D.3    Liu, J.4    Sessa, W.5
  • 12
    • 0024317054 scopus 로고
    • Tyrosine phosphorylation of a 22 kD protein is correlated with transformation with Rous sarcoma virus
    • Glenney J.R. Tyrosine phosphorylation of a 22 kD protein is correlated with transformation with Rous sarcoma virus. J. Biol. Chem. 264:1989;20163-20166.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20163-20166
    • Glenney, J.R.1
  • 13
    • 0026499749 scopus 로고
    • The sequence of human caveolin reveals identity with VIP 21, a component of transport vesicles
    • Glenney J.R. The sequence of human caveolin reveals identity with VIP 21, a component of transport vesicles. FEBS Lett. 314:1992;45-48.
    • (1992) FEBS Lett. , vol.314 , pp. 45-48
    • Glenney, J.R.1
  • 14
    • 0026454933 scopus 로고
    • Sequence and expression of caveolin, a protein component of caveolae plasma membrane domains phosphorylated on tyrosine in RSV-transformed fibroblasts
    • Glenney J.R., Soppet D. Sequence and expression of caveolin, a protein component of caveolae plasma membrane domains phosphorylated on tyrosine in RSV-transformed fibroblasts. Proc. Natl. Acad. Sci. USA. 89:1992;10517-10521.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10517-10521
    • Glenney, J.R.1    Soppet, D.2
  • 16
    • 0026640940 scopus 로고
    • VIP 21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles
    • Kurzchalia T., Dupree P., Parton R.G., Kellner R., Virta H., Lehnert M., Simons K. VIP 21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles. J. Cell Biol. 118:1992;1003-1014.
    • (1992) J. Cell Biol. , vol.118 , pp. 1003-1014
    • Kurzchalia, T.1    Dupree, P.2    Parton, R.G.3    Kellner, R.4    Virta, H.5    Lehnert, M.6    Simons, K.7
  • 17
    • 0029803093 scopus 로고    scopus 로고
    • Src tyrosine kinases, G alpha subunits and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases
    • Li S., Couet J., Lisanti M.P. Src tyrosine kinases, G alpha subunits and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases. J. Biol. Chem. 271:1996;29182-29190.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29182-29190
    • Li, S.1    Couet, J.2    Lisanti, M.P.3
  • 19
    • 0028285191 scopus 로고
    • Caveolae, caveolin and caveolin-rich membrane domains: A signalling hypothesis
    • Lisanti M.P., Scherer P., Tang Z.-L., Sargiacomo M. Caveolae, caveolin and caveolin-rich membrane domains: a signalling hypothesis. Trends Cell Biol. 4:1994;231-235.
    • (1994) Trends Cell Biol. , vol.4 , pp. 231-235
    • Lisanti, M.P.1    Scherer, P.2    Tang, Z.-L.3    Sargiacomo, M.4
  • 21
    • 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., Tang Z.-L., Sargiacomo M. Caveolin forms a hetero-oligomeric protein complex that interacts with an apical GPI-linked protein: implications for the biogenesis of caveolae. J. Cell Biol. 123:1993;595-604.
    • (1993) J. Cell Biol. , vol.123 , pp. 595-604
    • Lisanti, M.P.1    Tang, Z.-L.2    Sargiacomo, M.3
  • 22
    • 0028997529 scopus 로고
    • Caveolae purification and GPI-linked protein sorting in polarized epithelia
    • Lisanti M.P., Tang Z.-T., Scherer P., Sargiacomo M. Caveolae purification and GPI-linked protein sorting in polarized epithelia. Methods Enzymol. 250:1995;655-668.
    • (1995) Methods Enzymol. , vol.250 , pp. 655-668
    • Lisanti, M.P.1    Tang, Z.-T.2    Scherer, P.3    Sargiacomo, M.4
  • 23
  • 24
    • 0029879507 scopus 로고    scopus 로고
    • Localization of the PDGF-stimulated phosphorylation cascade to caveolae
    • Liu P., Ying Y., Ko Y.-G., Anderson R.G.W. Localization of the PDGF-stimulated phosphorylation cascade to caveolae. J. Biol. Chem. 271:1996;10299-10303.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10299-10303
    • Liu, P.1    Ying, Y.2    Ko, Y.-G.3    Anderson, R.G.W.4
  • 25
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins a family of scaffolding proteins for organizing pre-assembled signaling complexes at the plasma membrane
    • Okamoto T., Schlegel A., Scherer P.E., Lisanti M.P. Caveolins a family of scaffolding proteins for organizing pre-assembled signaling complexes at the plasma membrane. J. Biol. Chem. (Mini-Review). 273:1998;5419-5422.
    • (1998) J. Biol. Chem. (Mini-Review) , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 26
    • 0029014901 scopus 로고
    • Myryistoylation and differential palmitoylation of the HCK protein tyrosine kinases govern their attachment to membranes and association with caveolae
    • Robbins S.M., Quintrell N.A., Bishop M.J. Myryistoylation and differential palmitoylation of the HCK protein tyrosine kinases govern their attachment to membranes and association with caveolae. Mol. Cell. Biol. 15:1995;3507-3515.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3507-3515
    • Robbins, S.M.1    Quintrell, N.A.2    Bishop, M.J.3
  • 28
    • 0028108509 scopus 로고
    • In vitro phosphorylation of caveolin-rich membrane domains: Identification of an associated serine kinase activity as a casein kinase II-like enzyme
    • Sargiacomo M., Scherer P.E., Tang Z.-L., Casanova J.E., Lisanti M.P. In vitro phosphorylation of caveolin-rich membrane domains: identification of an associated serine kinase activity as a casein kinase II-like enzyme. Oncogene. 9:1994;2589-2595.
    • (1994) Oncogene , vol.9 , pp. 2589-2595
    • Sargiacomo, M.1    Scherer, P.E.2    Tang, Z.-L.3    Casanova, J.E.4    Lisanti, M.P.5
  • 29
    • 0027275642 scopus 로고
    • Signal transducing molecules and GPI-linked proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo M., Sudol M., Tang Z.-L., Lisanti M.P. Signal transducing molecules and GPI-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J. Cell Biol. 122:1993;789-807.
    • (1993) J. Cell Biol. , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.-L.3    Lisanti, M.P.4
  • 33
    • 0029003932 scopus 로고
    • Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution: Identification and epitope mapping of an isoform-specific monoclonal antibody probe
    • Scherer P.E., Tang Z.-L., Chun M.C., Sargiacomo M., Lodish H.F., Lisanti M.P. Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution: identification and epitope mapping of an isoform-specific monoclonal antibody probe. J. Biol. Chem. 270:1995;16395-16401.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16395-16401
    • Scherer, P.E.1    Tang, Z.-L.2    Chun, M.C.3    Sargiacomo, M.4    Lodish, H.F.5    Lisanti, M.P.6
  • 36
    • 0028175989 scopus 로고
    • Cysteine-3 of Src family tyrosine kinases determines palmitoylation and localization in caveolae
    • Shenoy-Scaria A.M., Dietzen D.J., Kwong J., Link D.C., Lublin D.M. Cysteine-3 of Src family tyrosine kinases determines palmitoylation and localization in caveolae. J. Cell Biol. 126:1994;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
  • 37
    • 0031054457 scopus 로고    scopus 로고
    • Reggie-1 and reggie-2, two cell surface proteins expressed by retinal ganglion cells during axon regeneration
    • Shulte T., Paschke K.A., Laessing U., Lottspeich F., Stuermer C.A. Reggie-1 and reggie-2, two cell surface proteins expressed by retinal ganglion cells during axon regeneration. Development. 124:1997;577-587.
    • (1997) Development , vol.124 , pp. 577-587
    • Shulte, T.1    Paschke, K.A.2    Laessing, U.3    Lottspeich, F.4    Stuermer, C.A.5
  • 38
    • 0002903772 scopus 로고
    • The cardiovascular system
    • In: Weiss, L. (Ed.) Elsevier Biomedical, New York
    • Simionescu, N., Simionsecu, M., 1983. The cardiovascular system. In: Weiss, L. (Ed.), Histology: Cell and Tissue Biology. Elsevier Biomedical, New York, pp. 371-433.
    • (1983) Histology: Cell and Tissue Biology , pp. 371-433
    • Simionescu, N.1    Simionsecu, M.2
  • 39
    • 0028125208 scopus 로고
    • Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation
    • Smart E., Ying Y.-S., Conrad P., Anderson R.G.W. Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation. J. Cell Biol. 127:1994;1185-1197.
    • (1994) J. Cell Biol. , vol.127 , pp. 1185-1197
    • Smart, E.1    Ying, Y.-S.2    Conrad, P.3    Anderson, R.G.W.4
  • 40
    • 0028820041 scopus 로고
    • A detergent free method for purifying caveolae membrane from tissue cultured cells
    • Smart E.J., Ying Y., Mineo C., Anderson R.G.W. A detergent free method for purifying caveolae membrane from tissue cultured cells. Proc. Natl. Acad. Sci. USA. 92:1995;10104-10108.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10104-10108
    • Smart, E.J.1    Ying, Y.2    Mineo, C.3    Anderson, R.G.W.4
  • 41
    • 0029912981 scopus 로고    scopus 로고
    • Copurification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent free purification of caveolae membranes
    • Song K.S., Li S., Okamoto T., Quilliam L., Sargiacomo M., Lisanti M.P. Copurification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent free purification of caveolae membranes. J. Biol. Chem. 271:1996;9690-9697.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9690-9697
    • Song, K.S.1    Li, S.2    Okamoto, T.3    Quilliam, L.4    Sargiacomo, M.5    Lisanti, M.P.6
  • 42
    • 15844401780 scopus 로고    scopus 로고
    • Expression of caveolin-3 in skeletal, cardiac and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins
    • Song K.S., Scherer P.E., Tang Z.-L., Okamoto T., Li S., Chafel M., Chu C., Kohtz D.S., Lisanti M.P. Expression of caveolin-3 in skeletal, cardiac and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins. J. Biol. Chem. 271:1996;15160-15165.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15160-15165
    • Song, K.S.1    Scherer, P.E.2    Tang, Z.-L.3    Okamoto, T.4    Li, S.5    Chafel, M.6    Chu, C.7    Kohtz, D.S.8    Lisanti, M.P.9
  • 43
    • 0031047967 scopus 로고    scopus 로고
    • Mutational analysis of the properties of caveolin-1. A novel role for the C-terminal domain in mediating homotypic caveolin-caveolin interactions
    • Song K.S., Tang Z.-L., Li S., Lisanti M.P. Mutational analysis of the properties of caveolin-1. A novel role for the C-terminal domain in mediating homotypic caveolin-caveolin interactions. J. Biol. Chem. 272:1997;4398-4403.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4398-4403
    • Song, K.S.1    Tang, Z.-L.2    Li, S.3    Lisanti, M.P.4
  • 44
    • 0031019022 scopus 로고    scopus 로고
    • Identification, sequence and expression of an invertebrate caveolin gene family from the nematode Caenorhabditis elegans. Implications for the molecular evolution of mammalian caveolin genes
    • Tang Z., Okamoto T., Boontrakulpoontawee P., Katada T., Otsuka A., Lisanti M. Identification, sequence and expression of an invertebrate caveolin gene family from the nematode Caenorhabditis elegans. Implications for the molecular evolution of mammalian caveolin genes. J. Biol. Chem. 272:1997;2437-2445.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2437-2445
    • Tang, Z.1    Okamoto, T.2    Boontrakulpoontawee, P.3    Katada, T.4    Otsuka, A.5    Lisanti, M.6
  • 46
    • 0024319520 scopus 로고
    • A non-radioactive in situ hybridization method for the localization of specific RNAs in Drosophila embryos reveals translational control of the segmentation gene hunchback
    • Tautz D., Pfeifle C. A non-radioactive in situ hybridization method for the localization of specific RNAs in Drosophila embryos reveals translational control of the segmentation gene hunchback. Chromosoma. 98:1989;81-85.
    • (1989) Chromosoma , vol.98 , pp. 81-85
    • Tautz, D.1    Pfeifle, C.2
  • 47
    • 0030561979 scopus 로고
    • M-caveolin, a muscle-specific caveolin-related protein
    • Way M., Parton R. M-caveolin, a muscle-specific caveolin-related protein. FEBS Lett. 376:1995;108-112.
    • (1995) FEBS Lett. , vol.376 , pp. 108-112
    • Way, M.1    Parton, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.