High impact information on COG2

• We have identified three new proteins that associate with Sec35p and Sec34p in yeast cytosol [1].
• Using a cell-free assay that measures distinct steps in vesicle transport from the ER to the Golgi, we find Sec35p is required for a vesicle docking stage catalyzed by Uso1p [2].
• The cold-sensitive lethality that results from deleting SEC35 is suppressed by YPT1 or SLY1-20 [2].
• These genetic and biochemical results suggest Sec35p acts with Uso1p to dock ER-derived vesicles to the Golgi complex [2].
• SEC35 encodes a novel cytosolic protein of 32 kD, peripherally associated with membranes [2].

Biological context of COG2

• The Saccharomyces cerevisiae proteins Sec34p and Sec35p are components of a large cytosolic complex involved in protein transport through the secretory pathway [3].
• Each of the eight genes that encode components of the Sec34p/sec35p complex was tested for its contribution to cell growth, protein transport, and the integrity of the complex [3].
• Missense mutations of SEC36 are lethal with mutations in COPI subunits, indicating a functional connection between the Sec34p/sec35p complex and the COPI vesicle coat [3].
• SEC35 was identified in a novel screen for temperature-sensitive mutants in the secretory pathway of the yeast Saccharomyces cerevisiae (. Genetics. 142:393-406) [2].

Anatomical context of COG2

• Sec34p, a protein required for vesicle tethering to the yeast Golgi apparatus, is in a complex with Sec35p [4].

Other interactions of COG2

• The sec31-sec35 mutants and additional alleles of previously identified sec and vacuolar protein sorting (vps) genes were isolated in a screen based on the detection of alpha-factor precursor in yeast colonies replicated to and lysed on nitrocellulose filters [5].
• Sgf1p, a new component of the Sec34p/Sec35p complex [6].

References