High impact information on SEC22

• By electron microscopy three of the mutants, sec18, sec17, and sec22, accumulate 50 nm vesicles at the nonpermissive temperature [1].
• Weaker suppression is evident upon overexpression of genes encoding the vesicle-SNAREs SEC22, BET1, or YKT6 [2].
• It forms a SNARE complex with Sec22 and the ER syntaxin Ufe1 [3].
• Sed5 is known to combine with two light chains (Bos1 and Sec22) to form the t-SNARE needed to receive vesicles from the endoplasmic reticulum [4].
• Sly1p-depleted cells, as well as a conditional lethal sly2 null mutant at nonpermissive temperatures, accumulate ER membranes and core-glycosylated invertase and carboxypeptidase Y [5].

Biological context of SEC22

• We isolated mutant yeast strains in which SEC22 gene function, which in a wild type strain background is non-essential for cell viability, has become essential [6].

Anatomical context of SEC22

• In vivo, AUT7 interacts genetically with endoplasmic reticulum to Golgi SNAREs, specifically with BET1 and SEC22 [7].
• We also identified a pattern of genetic interactions among these genes and another gene implicated in transport from the ER to the Golgi complex: SEC22 [8].
• SLY2 and SLY12 encode proteins with hydrophobic tails similar to synaptobrevins, integral membrane proteins of synaptic vesicles in higher eucaryotes [9].

Regulatory relationships of SEC22

• Moreover, overexpression of ISS1 could suppress mutations in SEC22 [10].

Other interactions of SEC22

• Deletion of ISS1 had no significant effect on growth or secretion; however, iss1Delta mutants were found to be synthetically lethal with mutations in the v-SNARE genes SEC22 and BET1 [10].
• In wild-type cells Kex2p-cleavage is observed only when Sec22-alpha is greatly overproduced [11].

Analytical, diagnostic and therapeutic context of SEC22

• Immunofluorescence microscopy and subcellular fractionation studies showed that Sec22-alpha is returned to the ER from the late Golgi (Kex2p) compartment [11].

References