Journal article
Bimodal Interaction of Coatomer with the p24 Family of Putative Cargo Receptors
Science (American Association for the Advancement of Science), Vol.273(5280), pp.1396-1399
09/06/1996
DOI: 10.1126/science.273.5280.1396
PMID: 8703076
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 α-, β'-, and ε-COP subunits of coatomer, whereas other p24 domains bound the β-, γ-, and ζ-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.
Details
- Title: Subtitle
- Bimodal Interaction of Coatomer with the p24 Family of Putative Cargo Receptors
- Creators
- Klaus Fiedler - Memorial Sloan Kettering Cancer CenterMichael Veit - Memorial Sloan Kettering Cancer CenterMark A. Stamnes - Memorial Sloan Kettering Cancer CenterJames E. Rothman - Memorial Sloan Kettering Cancer Center
- Resource Type
- Journal article
- Publication Details
- Science (American Association for the Advancement of Science), Vol.273(5280), pp.1396-1399
- DOI
- 10.1126/science.273.5280.1396
- PMID
- 8703076
- ISSN
- 0036-8075
- eISSN
- 1095-9203
- Language
- English
- Date published
- 09/06/1996
- Academic Unit
- Molecular Physiology and Biophysics; Internal Medicine
- Record Identifier
- 9984297605302771
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