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. 2010 Aug 9;190(3):331–345. doi: 10.1083/jcb.201003005

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© 2010 Ong et al.

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Figure 8. — p125A stabilizes the Sec13/Sec31 heterotetramer to the ERES membrane. (A) Membrane (m) and cytosol (c) fractions were obtained from cells transfected with siRNA. Equivalent amounts of each fraction were subjected to SDS-PAGE followed by immunoblot analysis. Molecular size markers are in kD. The intensities of the bands were quantified using Quantity One software (Bio-Rad Laboratories). The ratio of distribution is relative to the total. Total = m (membrane fraction) + c (cytosol fraction). Ratio = m or c/(m+c). The experiment was repeated three times; *, P < 0.05. Syntaxin 6 (Syn6) was used as the marker for the membrane fraction and the Rho GDP dissociation inhibitor (RhoGDI) was used as the marker for the cytosolic fraction. (B) A working model to illustrate the role of p125A in ER export in mammalian cells. The majority of p125A, Sec31A, and Sec13 likely exists in the form of a heterohexamer. Upon recruitment of Sar1 and Sec23A/Sec24 subcomplex during COPII vesicle budding, the p125A/Sec31A/Sec13 subcomplex is then recruited, which may open up the binding site of p125A for Sec23A. The simultaneous interaction of p125A with both Sec31A and Sec23A on the budding vesicles may facilitate the coordination of these two COPII subcomplexes to mediate vesicle formation.