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Published online
doi:10.1083/jcb.200903053
The Journal of Cell Biology, Vol. 185, No. 7, 1259-1273
The Rockefeller University Press, 0021-9525 $30.00
© Bastiani et al.
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Article

MURC/Cavin-4 and cavin family members form tissue-specific caveolar complexes



Michele Bastiani1, Libin Liu4, Michelle M. Hill1, Mark P. Jedrychowski4, Susan J. Nixon1, Harriet P. Lo1, Daniel Abankwa1, Robert Luetterforst1, Manuel Fernandez-Rojo1, Michael R. Breen4, Steven P. Gygi5, Jorgen Vinten6, Piers J. Walser1, Kathryn N. North3, John F. Hancock1, Paul F. Pilch4, and Robert G. Parton1,2

1 Institute for Molecular Bioscience and 2 Center for Microscopy and Microanalysis, The University of Queensland, Brisbane, Queensland 4072, Australia
3 Institute for Neuromuscular Research, The Children's Hospital at Westmead, Sydney, New South Wales 2145, Australia
4 Department of Biochemistry, Boston University School of Medicine, Boston, MA 02118
5 Department of Cell Biology, Harvard Medical School, Boston, MA 02115
6 Department of Medical Physiology, The Panum Institute, University of Copenhagen, Copenhagen N 2200, Denmark

Correspondence to Robert G. Parton: R.Parton{at}imb.uq.edu.au

Polymerase I and transcript release factor (PTRF)/Cavin is a cytoplasmic protein whose expression is obligatory for caveola formation. Using biochemistry and fluorescence resonance energy transfer–based approaches, we now show that a family of related proteins, PTRF/Cavin-1, serum deprivation response (SDR)/Cavin-2, SDR-related gene product that binds to C kinase (SRBC)/Cavin-3, and muscle-restricted coiled-coil protein (MURC)/Cavin-4, forms a multiprotein complex that associates with caveolae. This complex can constitutively assemble in the cytosol and associate with caveolin at plasma membrane caveolae. Cavin-1, but not other cavins, can induce caveola formation in a heterologous system and is required for the recruitment of the cavin complex to caveolae. The tissue-restricted expression of cavins suggests that caveolae may perform tissue-specific functions regulated by the composition of the cavin complex. Cavin-4 is expressed predominantly in muscle, and its distribution is perturbed in human muscle disease associated with Caveolin-3 dysfunction, identifying Cavin-4 as a novel muscle disease candidate caveolar protein.

M. Bastiani, L. Liu, P.F. Pilch, and R.G. Parton contributed equally to this paper.

J.F. Hancock's present address is Dept. of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, Houston, TX 77030

Abbreviations used in this paper: Cav1, Caveolin-1; Cav3, Caveolin-3; FLIM, fluorescence lifetime imaging microscopy; FRET, fluorescence resonance energy transfer; iMEF, immortalized mouse embryonic fibroblast; MURC, muscle-restricted coiled-coil protein; PS, phosphatidylserine; PTRF, polymerase I and transcript release factor; SDR, serum deprivation response; shRNA, short hairpin RNA; SRBC, SDR-related gene product that binds to C kinase; WT, wild type.

© 2009 Bastiani et al.
This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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