Bastiani, MicheleLiu, LibinHill, Michelle M.Jedrychowski, Mark P.Nixon, Susan J.Lo, Harriet P.Abankwa, DanielLuetterforst, RobertFernandez-Rojo, ManuelBreen, Michael R.Gygi, Steven P.Vinten, JorgenWalser, Piers J.North, Kathryn N.Hancock, John F.Pilch, Paul F.Parton, Robert G.2012-01-112012-01-1120092009-06-22Bastiani, Michele, Libin Liu, Michelle M. Hill, Mark P. Jedrychowski, Susan J. Nixon, Harriet P. Lo, Daniel Abankwa, Robert Luetterforst, Manuel Fernandez-Rojo, Michael R. Breen, Steven P. Gygi, Jorgen Vinten, Piers J. Walser, Kathryn N. North, John F. Hancock, Paul F. Pilch, Robert G. Parton. "MURC/Cavin-4 and cavin family members form tissue-specific caveolar complexes" Journal of Cell Biology 185(7): 1259-1273. (2009)1540-8140https://hdl.handle.net/2144/3220Polymerase 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.enCopyright 2009 Bastiani et al.http://creativecommons.org/licenses/by/2.0/Article10.1083/jcb.200903053195462422712963