Autor: |
Alberto T Gatta, Louise H Wong, Yves Y Sere, Diana M Calderón-Noreña, Shamshad Cockcroft, Anant K Menon, Tim P Levine |
Jazyk: |
angličtina |
Rok vydání: |
2015 |
Předmět: |
|
Zdroj: |
eLife, Vol 4 (2015) |
Druh dokumentu: |
article |
ISSN: |
2050-084X |
DOI: |
10.7554/eLife.07253 |
Popis: |
Sterol traffic between the endoplasmic reticulum (ER) and plasma membrane (PM) is a fundamental cellular process that occurs by a poorly understood non-vesicular mechanism. We identified a novel, evolutionarily diverse family of ER membrane proteins with StART-like lipid transfer domains and studied them in yeast. StART-like domains from Ysp2p and its paralog Lam4p specifically bind sterols, and Ysp2p, Lam4p and their homologs Ysp1p and Sip3p target punctate ER-PM contact sites distinct from those occupied by known ER-PM tethers. The activity of Ysp2p, reflected in amphotericin-sensitivity assays, requires its second StART-like domain to be positioned so that it can reach across ER-PM contacts. Absence of Ysp2p, Ysp1p or Sip3p reduces the rate at which exogenously supplied sterols traffic from the PM to the ER. Our data suggest that these StART-like proteins act in trans to mediate a step in sterol exchange between the PM and ER. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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