Palmitoylation of prohibitin at cysteine 69 facilitates its membrane translocation and interaction with Eps 15 homology domain protein 2 (EHD2).
Plasma membrane translocation of specific cytosolic proteins plays an important role in cell signaling pathways. We have recently shown that prohibitin (PHB) , a protein present in the plasma membranes of various cell types, interacts with Eps 15 homology domain protein 2 (EHD2), a lipid raft protein. However, the mechanism involved in membrane translocation of PHB is not known.We report that PHB undergoes palmitoylation at cysteine 69 (Cys69), and that this palmitoylation is required for PHB's membrane translocation. Furthermore, we demonstrate that membrane translocation of PHB facilitates tyrosine phosphorylation and its interaction with EHD2. Thus, the palmitoylation and membrane translocation of PHB and its interaction with EHD2 may play a role in cell signaling.
Ande
Sudharsana Rao
SR
Department of Internal Medicine, University of Manitoba, 843 John Buhler Research Centre, 715 McDermot Ave., Winnipeg, MB R3E 3P4, Canada.
Mishra
Suresh
S
D000595:Amino Acid Sequence; D015153:Blotting, Western; D002352:Carrier Proteins / Q000378:metabolism*; D002478:Cells, Cultured; D003545:Cysteine / Q000378:metabolism; D006801:Humans; D047468:Immunoprecipitation; D054878:Lipoylation; D021962:Membrane Microdomains / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D000091402:Prohibitins; D021381:Protein Transport; D012097:Repressor Proteins / Q000737:chemistry / Q000378:metabolism*
D002352:Carrier Proteins; C406446:EHD2 protein, human; D008565:Membrane Proteins; C000717328:PHB protein, human; D000091402:Prohibitins; D012097:Repressor Proteins; D003545:Cysteine