Rab5 is necessary for the biogenesis of the endolysosomal system in vivo (Q39294010)

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scientific article published on 23 May 2012

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English	Rab5 is necessary for the biogenesis of the endolysosomal system in vivo	scientific article published on 23 May 2012

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PubMed publication ID

22622570

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10 September 2017

title

Rab5 is necessary for the biogenesis of the endolysosomal system in vivo (English)

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10 September 2017

author

Jerome Gilleron

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2

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Yannis Kalaidzidis

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13

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Yannis Kalaidzidis

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Victor E. Koteliansky

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Victor Koteliansky

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Anja Zeigerer

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Roman L Bogorad

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3

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Giovanni Marsico

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Hidenori Nonaka

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Sarah Seifert

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Hila Epstein-Barash

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Satya Kuchimanchi

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Chang Geng Peng

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Vera M Ruda

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Perla Del Conte-Zerial

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Jan G Hengstler

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Marino Zerial

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15

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10 September 2017

language of work or name

English

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publication date

23 May 2012

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22622570

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10 September 2017

published in

Nature

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volume

485

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issue

7399

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10 September 2017

page(s)

465-470

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Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface.

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Rab7 associates with early endosomes to mediate sorting and transport of Semliki forest virus to late endosomes

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Co-operative regulation of endocytosis by three Rab5 isoforms

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rab5 controls early endosome fusion in vitro

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Rab conversion as a mechanism of progression from early to late endosomes

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Intracellular trafficking of bile salt export pump (ABCB11) in polarized hepatic cells: constitutive cycling between the canalicular membrane and rab11-positive endosomes

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The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway

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Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin

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Endocytosis

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Differential involvement of endocytic compartments in the biosynthetic traffic of apical proteins

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Mutations in human dynamin block an intermediate stage in coated vesicle formation

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Sequential roles for phosphatidylinositol 3-phosphate and Rab5 in tethering and fusion of early endosomes via their interaction with EEA1

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The Rab5 effector EEA1 is a core component of endosome docking

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Constitutive activated Cdc42-associated kinase (Ack) phosphorylation at arrested endocytic clathrin-coated pits of cells that lack dynamin

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Transformational process of the endosomal compartment in nephrocytes of Drosophila melanogaster

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Rab11a and myosin Vb are required for bile canalicular formation in WIF-B9 cells

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Rab13 regulates membrane trafficking between TGN and recycling endosomes in polarized epithelial cells.

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Membrane transport in the endocytic pathway

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Small GTPase Rab5 participates in chromosome congression and regulates localization of the centromere-associated protein CENP-F to kinetochores

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Targeted delivery of RNAi therapeutics with endogenous and exogenous ligand-based mechanisms

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GTPase activity of Rab5 acts as a timer for endocytic membrane fusion

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Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells

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Membrane identity and GTPase cascades regulated by toggle and cut-out switches

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Endocytosis and molecular sorting

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Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes.

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Role of Drosophila Rab5 during endosomal trafficking at the synapse and evoked neurotransmitter release

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Rab5 isoforms differentially regulate the trafficking and degradation of epidermal growth factor receptors

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Unsolved mysteries in membrane traffic

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Apical plasma membrane proteins and endolyn-78 travel through a subapical compartment in polarized WIF-B hepatocytes.

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Membrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cells

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Hepatic metabolism of colloidal gold-low-density lipoprotein complexes in the rat: evidence for bulk excretion of lysosomal contents into bile

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Identification of the switch in early-to-late endosome transition

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Regulation of early endosomal entry by the Drosophila tumor suppressors Rabenosyn and Vps45.

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The maintenance and generation of membrane polarity in hepatocytes

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Systems survey of endocytosis by multiparametric image analysis.

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Identifiers

DOI

10.1038/NATURE11133

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Europe PubMed Central

PubMed publication ID

22622570

retrieved

10 September 2017

PubMed publication ID

22622570

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stated in

Europe PubMed Central

PubMed publication ID

22622570

retrieved

10 September 2017

ResearchGate publication ID

225058595

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