Galectins CLIC cargo inside

Pamela Stanley

doi:10.1038/ncb2983

Galectins CLIC cargo inside

Pamela Stanley

Cell Biology

Research output: Contribution to journal › Review article › peer-review

9 Scopus citations

Abstract

Clathrin-independent endocytosis removes membrane receptors and other proteins from the cell surface, yet the mechanisms controlling this process remain unclear. Galectin-3 is now shown to regulate the biogenesis of a subpopulation of clathrin-independent carriers (CLICs). Galectin-3 binds to glycosylated cargo proteins and interacts with membrane glycosphingolipids to induce membrane deformation and CLIC formation.

Original language	English (US)
Pages (from-to)	506-507
Number of pages	2
Journal	Nature Cell Biology
Volume	16
Issue number	6
DOIs	https://doi.org/10.1038/ncb2983
State	Published - Jun 2014

ASJC Scopus subject areas

Cell Biology

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10.1038/ncb2983

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title = "Galectins CLIC cargo inside",

abstract = "Clathrin-independent endocytosis removes membrane receptors and other proteins from the cell surface, yet the mechanisms controlling this process remain unclear. Galectin-3 is now shown to regulate the biogenesis of a subpopulation of clathrin-independent carriers (CLICs). Galectin-3 binds to glycosylated cargo proteins and interacts with membrane glycosphingolipids to induce membrane deformation and CLIC formation.",

author = "Pamela Stanley",

year = "2014",

month = jun,

doi = "10.1038/ncb2983",

language = "English (US)",

volume = "16",

pages = "506--507",

journal = "Nature Cell Biology",

issn = "1465-7392",

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AU - Stanley, Pamela

PY - 2014/6

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N2 - Clathrin-independent endocytosis removes membrane receptors and other proteins from the cell surface, yet the mechanisms controlling this process remain unclear. Galectin-3 is now shown to regulate the biogenesis of a subpopulation of clathrin-independent carriers (CLICs). Galectin-3 binds to glycosylated cargo proteins and interacts with membrane glycosphingolipids to induce membrane deformation and CLIC formation.

AB - Clathrin-independent endocytosis removes membrane receptors and other proteins from the cell surface, yet the mechanisms controlling this process remain unclear. Galectin-3 is now shown to regulate the biogenesis of a subpopulation of clathrin-independent carriers (CLICs). Galectin-3 binds to glycosylated cargo proteins and interacts with membrane glycosphingolipids to induce membrane deformation and CLIC formation.

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DO - 10.1038/ncb2983

M3 - Review article

C2 - 24875739

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VL - 16

SP - 506

EP - 507

JO - Nature Cell Biology

JF - Nature Cell Biology

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ER -

Galectins CLIC cargo inside

Abstract

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