Bimodal interaction of coatomer with the p24 family of putative cargo receptors.
Cytoplasmic domains of members of the p24 family of putative cargo receptors were shown to bind to coatomer, the coat protein of COPI-coated transport vesicles. Domains that contained dilysine endoplasmic reticulum retrieval signals bound the alpha-, beta'-, and epsilon-COP subunits of coatomer, whereas other p24 domains bound the beta-, gamma-, and zeta-COP subunits and required a phenylalanine-containing motif. Transit of a CD8-p24 chimera from the endoplasmic reticulum through the Golgi complex was slowed when the phenylalanine motif was mutated, suggesting that this motif may function as an anterograde transport signal. The either-or bimodal binding of coatomer to p24 tails suggests models for how coatomer can potentially package retrograde-directed and anterograde-directed cargo into distinct COPI-coated vesicles.
Fiedler
K
K
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA.
Veit
M
M
Stamnes
M A
MA
Rothman
J E
JE
D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport; D016466:CHO Cells; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D018699:Coated Vesicles / Q000378:metabolism*; D020756:Coatomer Protein; D006224:Cricetinae; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism; D008239:Lysine / Q000032:analysis; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D009685:Nuclear Envelope / Q000378:metabolism; D010649:Phenylalanine / Q000032:analysis; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D002352:Carrier Proteins; D020756:Coatomer Protein; D008565:Membrane Proteins; D011993:Recombinant Fusion Proteins; D010649:Phenylalanine; D008239:Lysine