High impact information on SUR7

• Plasma membrane depolarization causes reversible dispersion of the H(+)-symporters, not however of the Sur7 protein [1].
• SUR7 was originally described as a multicopy suppressor of rvs167, whose product is an actin patch component [2].
• Digestion of the cell wall caused Sur7p patches to disassemble, indicating that Sur7p requires cell wall-dependent extracellular interactions for its localization as patches. sur7Delta, ydl222Delta, and ynl194Delta mutants had reduced sporulation efficiencies [2].
• Cloning of the multicopy suppressor gene SUR7: evidence for a functional relationship between the yeast actin-binding protein Rvs167 and a putative membranous protein [3].
• We showed that the suppressive ability of the overexpressed SUR7 gene concerns all the rvs167 phenotypes [3].

Anatomical context of SUR7

• This suppression is probably mediated by sphingolipids, since deletion of SUR7, YDL222, and YNL194 altered the sphingolipid content of the yeast plasma membrane, and other SUR genes suppress rvs167 via effects on sphingolipid synthesis [2].

Other interactions of SUR7

• The four transmembrane-span proteins Sur7p and Nce102p were also present in the isolated plasma membranes, as well as the unknown protein Ygr266wp that probably contains a single transmembrane span [4].

References