SRBC/cavin-3 is a caveolin adapter protein that regulates caveolae function

Kerrie Ann McMahon, Hubert Zajicek, Wei Ping Li, Michael J. Peyton, John D. Minna, V. James Hernandez, Katherine Luby-Phelps, Richard G W Anderson

Research output: Contribution to journalArticlepeer-review

162 Scopus citations


Caveolae are a major membrane domain common to most cells. One of the defining features of this domain is the protein caveolin. The exact function of caveolin, however, is not clear. One possible function is to attract adapter molecules to caveolae in a manner similar to how clathrin attracts molecules to coated pits. Here, we characterize a candidate adapter molecule called SRBC. SRBC binds PKC and is a member of the STICK (substrates that interact with C-kinase) superfamily of PKC-binding proteins. We also show it co-immunoprecipitates with caveolin-1. A leucine zipper in SRBC is essential for both co-precipitation with caveolin and localization to caveolae. SRBC remains associated with caveolin when caveolae bud to form vesicles (cavicles) that travel on microtubules to different regions of the cell. In the absence of SRBC, intracellular cavicle traffic is markedly impaired. We conclude that SRBC (sdr-related gene product that binds to c-kinase) and two other family members PTRF (Pol I and transcription release factor) and SDPR function as caveolin adapter molecules that regulate caveolae function.

Original languageEnglish (US)
Pages (from-to)1001-1015
Number of pages15
JournalEMBO Journal
Issue number8
StatePublished - Apr 22 2009


  • Adapter protein
  • Caveolae
  • Caveolin
  • endocytosis

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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