Depletion of β-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1

• DOI: 10.1152/ajpcell.00010.2008
• Publication Date: 2008-04-03T01:10:54Z
• Authors: Melanie L. Styers; Amber K. O'Connor; Robert Grabski; Estelle Cormet-Bo...; Elizabeth Sztul
• Keywords: COPI; COPII; Compartmentalization (fire protection); Transport protein; Cellular compartment; Compartment (ship)

We have utilized small interfering RNA (siRNA)-mediated depletion of the β-COP subunit COP-I to explore function in organellar compartmentalization and protein traffic. Reduction levels causes colocalization markers for endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN), recycling endosomes large, globular compartments. The lack spatial differentiation these compartments is not due a general collapse all cellular organelles since early lysosomes do redistribute common structures. Anterograde trafficking transmembrane cargo vesicular stomatitis virus membrane glycoprotein subset soluble cargoes arrested within Similarly, traffic transferrin through perturbed. Furthermore, caveolin-1 (Cav1), structural caveolae, Importantly, Cav1 coprecipitates with γ-subunit COP-I, suggesting that cargo. Our findings suggest required ERGIC, TGN, plays novel role biosynthetic transport Cav1.