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p24 and p23, the major transmembrane proteins of COPI‐coated transport vesicles, form hetero‐oligomeric complexes and cycle between the organelles of the early secretory pathway
Author(s) -
Gommel D,
Orci L,
Emig E.M,
Hannah M.J,
Ravazzola M,
Nickel W,
Helms J.B,
Wieland F.T,
Sohn K
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00246-x
Subject(s) - copi , golgi apparatus , vesicle , microbiology and biotechnology , organelle , secretory pathway , copii , golgi membrane , chemistry , biophysics , biology , endoplasmic reticulum , membrane , biochemistry
COPI‐coated vesicles that bud off the Golgi complex contain two major transmembrane proteins, p23 and p24. We have localized the protein at the Golgi complex and at COPI‐coated vesicles. Transport from the intermediate compartment (IC) to the Golgi can be blocked at 15°C, and under these conditions p24 accumulates in peripheral punctated structures identified as IC. Release from the temperature block leads to a redistribution of p24 to the Golgi, showing that p24, similar to p23, cycles between the IC and Golgi complex. Immunoprecipitations of p24 from cell lysates and from detergent‐solubilized Golgi membranes and COPI‐coated vesicles show that p24 and p23 interact with each other to form a complex. Transient transfection of p23 in HeLa cells shows that p23 and p24 colocalize in structures induced by the overexpression of p23. Taken together p24 interacts with p23 and constitutively cycles between the organelles of the early secretory pathway.