PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER–plasma membrane contacts | Zendy

Jeeyun Chung | Zendy; Federico Torta | Zendy; Kaori Masai | Zendy; Louise Lucast | Zendy; Heather Czapla | Zendy; Lukas B. Tanner | Zendy; Pradeep Narayanaswamy | Zendy; Markus R. Wenk | Zendy; Fubito Nakatsu | Zendy; Pietro De Camilli | Zendy

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PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER–plasma membrane contacts

Author(s) -

Jeeyun Chung,

Federico Torta,

Kaori Masai,

Louise Lucast,

Heather Czapla,

Lukas B. Tanner,

Pradeep Narayanaswamy,

Markus R. Wenk,

Fubito Nakatsu,

Pietro De Camilli

Publication year - 2015

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aab1370

Subject(s) - membrane contact site , endoplasmic reticulum , phosphatidylserine , organelle , phospholipid , membrane , phospholipid scramblase , microbiology and biotechnology , chemistry , membrane protein , biochemistry , biology , integral membrane protein

Membrane contact sites promote lipid exchange Most membrane lipids are manufactured in the endoplasmic reticulum (ER). Different organelles and the plasma membrane (PM) have distinct phospholipid compositions. Chunget al. , working in mammalian cells, and Moser von Filsecket al. , working in yeast, both describe how a family of proteins is important in maintaining the balance of lipids within the cell. These special proteins accumulate at and tether contact sites between the ER and the PM and promote the exchange of specific phospholipids, which helps to maintain the PM's distinct identity.Science , this issue pp.428 and432

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