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J Biol Chem, Vol. 274, Issue 36, 25718-25725, September 3, 1999
From the Departments of a Molecular Pharmacology and
g Cell Biology, Albert Einstein College of Medicine, Bronx, New
York 10461, the b Department of Hematology-Oncology, Istituto
Superiore di Sanità, 00161 Rome, Italy, the c Istituto di
Medicina Interna e Scienze Oncologiche, Perugina University, 06100 Perugina, Italy, the e Department of Neurosciences, The Lerner
Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, i Dyson Vision Research Institute, Weill Medical College of
Cornell University, New York, New York 10021, and the k Kimmel
Cancer Center, Thomas Jefferson University,
Philadelphia, Pennsylvania 19107
Caveolins-1 and -2 are normally co-expressed, and
they form a hetero-oligomeric complex in many cell types. These
caveolin hetero-oligomers are thought to represent the assembly units
that drive caveolae formation in vivo. However, the
functional significance of the interaction between caveolins-1 and -2 remains unknown. Here, we show that caveolin-1 co-expression is
required for the transport of caveolin-2 from the Golgi complex to the
plasma membrane. We identified a human erythroleukemic cell line, K562,
that expresses caveolin-2 but fails to express detectable levels of
caveolin-1. This allowed us to stringently assess the effects of
recombinant caveolin-1 expression on the behavior of endogenous
caveolin-2. We show that expression of caveolin-1 in K562 cells is
sufficient to reconstitute the de novo formation of
caveolae in these cells. In addition, recombinant expression of
caveolin-1 allows caveolin-2 to form high molecular mass oligomers that
are targeted to caveolae-enriched membrane fractions. In striking
contrast, in the absence of caveolin-1 expression, caveolin-2 forms low
molecular mass oligomers that are retained at the level of the Golgi
complex. Interestingly, we also show that expression of caveolin-1 in
K562 cells dramatically up-regulates the expression of endogenous
caveolin-2. Northern blot analysis reveals that caveolin-2
mRNA levels remain constant under these conditions,
suggesting that the expression of caveolin-1 stabilizes the
caveolin-2 protein. Conversely, transient expression of caveolin-2 in
CHO cells is sufficient to up-regulate endogenous caveolin-1
expression. Thus, the formation of a hetero-oligomeric complex between
caveolins-1 and -2 stabilizes the caveolin-2 protein product and allows
caveolin-2 to be transported from the Golgi complex to the plasma membrane.
Expression of Caveolin-1 Is Required for the Transport of
Caveolin-2 to the Plasma Membrane
RETENTION OF CAVEOLIN-2 AT THE LEVEL OF THE GOLGI COMPLEX
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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 A. A. Zamyatnin Jr,, A. G. Solovyev, A. A. Sablina, A. A. Agranovsky, L. Katul, H. J. Vetten, J. Schiemann, A. E. Hinkkanen, K. Lehto, and S. Yu. Morozov Dual-colour imaging of membrane protein targeting directed by poa semilatent virus movement protein TGBp3 in plant and mammalian cells J. Gen. Virol., March 1, 2002; 83(3): 651 - 662. [Abstract] [Full Text] [PDF]
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L. Breuza, S. Corby, J.-P. Arsanto, M.-H. Delgrossi, P. Scheiffele, and A. Le Bivic The scaffolding domain of caveolin 2 is responsible for its Golgi localization in Caco-2 cells J. Cell Sci., January 12, 2002; 115(23): 4457 - 4467. [Abstract] [Full Text] [PDF]
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H. Lee, D. Volonte’, F. Galbiati, P. Iyengar, D. M. Lublin, D. B. Bregman, M. T. Wilson, R. Campos-Gonzalez Boumediene Bouzahzah, R. G. Pestell, P. E. Scherer, et al. Constitutive and Growth Factor-Regulated Phosphorylation of Caveolin-1 Occurs at the Same Site (Tyr-14) in Vivo: Identification of a c-Src/Cav-1/Grb7 Signaling Cassette Mol. Endocrinol., November 1, 2000; 14(11): 1750 - 1775. [Abstract] [Full Text]
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T Fujimoto, H Kogo, R Nomura, and T Une Isoforms of caveolin-1 and caveolar structure J. Cell Sci., January 10, 2000; 113(19): 3509 - 3517. [Abstract] [PDF]
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E. J. Smart, G. A. Graf, M. A. McNiven, W. C. Sessa, J. A. Engelman, P. E. Scherer, T. Okamoto, and M. P. Lisanti Caveolins, Liquid-Ordered Domains, and Signal Transduction Mol. Cell. Biol., November 1, 1999; 19(11): 7289 - 7304. [Full Text] [PDF]
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H. Lee, S. E. Woodman, J. A. Engelman, D. Volonte', F. Galbiati, H. L. Kaufman, D. M. Lublin, and M. P. Lisanti Palmitoylation of Caveolin-1 at a Single Site (Cys-156) Controls Its Coupling to the c-Src Tyrosine Kinase. TARGETING OF DUALLY ACYLATED MOLECULES (GPI-LINKED, TRANSMEMBRANE, OR CYTOPLASMIC) TO CAVEOLAE EFFECTIVELY UNCOUPLES c-Src AND CAVEOLIN-1 (TYR-14) J. Biol. Chem., September 7, 2001; 276(37): 35150 - 35158. [Abstract] [Full Text] [PDF]
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B. Razani, J. A. Engelman, X. B. Wang, W. Schubert, X. L. Zhang, C. B. Marks, F. Macaluso, R. G. Russell, M. Li, R. G. Pestell, et al. Caveolin-1 Null Mice Are Viable but Show Evidence of Hyperproliferative and Vascular Abnormalities J. Biol. Chem., October 5, 2001; 276(41): 38121 - 38138. [Abstract] [Full Text] [PDF]
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