Abstract
Coiled-coil proteins of the golgin family have been implicated in intra-Golgi transport through tethering coat protein complex I (COPI) vesicles. The p115-golgin tether is the best studied, and here we characterize the golgin-84-CASP tether. The vesicles bound by this tether were strikingly different from those bound by the p115-golgin tether in that they lacked members of the p24 family of putative cargo receptors and contained enzymes instead of anterograde cargo. Microinjected golgin-84 or CASP also inhibited Golgi-enzyme transport to the endoplasmic reticulum, further implicating this tether in retrograde transport. These and other golgins may modulate the flow patterns within the Golgi stack.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Animals
-
Autoantigens / metabolism*
-
Binding, Competitive
-
COP-Coated Vesicles / metabolism*
-
Cell Fractionation
-
Cell Line
-
Cytoskeletal Proteins / metabolism*
-
DNA-Binding Proteins
-
Endoplasmic Reticulum / metabolism
-
Golgi Apparatus / chemistry
-
Golgi Apparatus / enzymology
-
Golgi Apparatus / metabolism*
-
Golgi Matrix Proteins
-
Humans
-
Immunoprecipitation
-
Membrane Glycoproteins / metabolism
-
Membrane Proteins / metabolism*
-
Microscopy, Electron
-
Protein Transport
-
Rats
-
Recombinant Fusion Proteins / metabolism
-
Transcription Factors
-
Viral Envelope Proteins / metabolism
Substances
-
Autoantigens
-
Cux1 protein, rat
-
Cytoskeletal Proteins
-
DNA-Binding Proteins
-
G protein, vesicular stomatitis virus
-
Golgi Matrix Proteins
-
Membrane Glycoproteins
-
Membrane Proteins
-
Recombinant Fusion Proteins
-
Transcription Factors
-
Viral Envelope Proteins
-
golgin-84, rat
-
macrogolgin