Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Biological Transport
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CHO Cells
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism*
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Cell Membrane / metabolism
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Coated Vesicles / metabolism*
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Coatomer Protein
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Cricetinae
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Endoplasmic Reticulum / metabolism
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Golgi Apparatus / metabolism
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Lysine / analysis
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism*
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Molecular Sequence Data
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Nuclear Envelope / metabolism
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Phenylalanine / analysis
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Recombinant Fusion Proteins / metabolism
Substances
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Carrier Proteins
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Coatomer Protein
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Membrane Proteins
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Recombinant Fusion Proteins
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Phenylalanine
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Lysine
Associated data
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GENBANK/F06012
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GENBANK/F07445
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GENBANK/L22015
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GENBANK/R14234
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GENBANK/R25915
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GENBANK/T11000
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GENBANK/T17481
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GENBANK/T27339
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GENBANK/T27390
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GENBANK/T32238
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GENBANK/T34121
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GENBANK/T36996
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GENBANK/T46519
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GENBANK/T48545
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GENBANK/T48838
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GENBANK/T98284
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GENBANK/U00059
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GENBANK/U26264
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GENBANK/X53592
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GENBANK/X67317
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GENBANK/X87331
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GENBANK/Z34726
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GENBANK/Z48432
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GENBANK/Z49810