The primary sequence of murine caveolin reveals a conserved consensus site for phosphorylation by protein kinase C.
We report here the cloning of the murine cDNA encoding caveolin, a known v-Src substrate and caveolar marker protein. Interestingly, analysis of the murine cDNA and comparison with caveolin from other species reveals a previously unrecognized consensus site for protein kinase C (PKC) phosphorylation. This finding could have important implications as (i) both the morphology and function of caveolae are dramatically affected by PKC activators; and (ii) PKC alpha is concentrated in isolated caveolin-rich membrane domains. In addition, this first step should facilitate the use of the mouse as a genetic system for elucidating the role of caveolin in caveolar functioning.
Tang
Z L
ZL
Whitehead Institute for Biomedical Research, Cambridge MA 02142-1479.
Scherer
P E
PE
Lisanti
M P
MP
D000595:Amino Acid Sequence; D000818:Animals; D051242:Caveolin 1; D022461:Caveolins; D003001:Cloning, Molecular; D017124:Conserved Sequence; D018076:DNA, Complementary; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
C495540:CAV1 protein, human; C495541:Cav1 protein, mouse; D051242:Caveolin 1; D022461:Caveolins; D018076:DNA, Complementary; D008565:Membrane Proteins; D011493:Protein Kinase C