© John Wiley & Sons A/S. Published by John Wiley & Sons Ltd
Edited By: Michael S. Marks, Trina A. Schroer, Tom H. Stevens, Sharon A. Tooze
Online ISSN: 1600-0854
ORIGINAL ARTICLE: Distinct Trafficking of Cell Surface and Endosomal TIM-1 to the Immune Synapse
ORIGINAL ARTICLE: A Cholesterol-Dependent Endocytic Mechanism Generates Midbody Tubules During Cytokinesis
ORIGINAL ARTICLE: Distinct Temporal Regulation of RET Isoform Internalization: Roles of Clathrin and AP2
ORIGINAL ARTICLE: Endocytosis of Ubiquitylation-Deficient EGFR Mutants via Clathrin-Coated Pits is Mediated by Ubiquitylation
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Recruitment of VPS33A to HOPS by VPS16 Is Required for Lysosome Fusion with Endosomes and Autophagosomes
Lena Wartosch, Ufuk Günesdogan, Stephen C. Graham and J. Paul Luzio
Article first published online: 30 APR 2015 | DOI: 10.1111/tra.12283
In yeast the homotypic fusion and vacuole protein sorting (HOPS) complex is a tether required for vacuole fusion. We show that all proteins of the mammalian HOPS complex are necessary for fusion of lysosomes with endosomes and that recruitment of the Sec1/Munc18 (SM) protein VPS33A to the complex via VPS16 is essential for this and for fusion of lysosomes with autophagosomes. Mammalian VPS33B and VIPAR are not required for these fusion events and are not part of the HOPS or the class C core vacuole/endosome tethering (CORVET) complexes, but form a separate complex.
Rab5 and Ndfip1 Are Involved in Pten Ubiquitination and Nuclear Trafficking
Yijia Li, Ley-Hian Low, Ulrich Putz, Choo-Peng Goh, Seong-Seng Tan and Jason Howitt
Depending on its localization, Pten (the central antagonist of PI3K signaling in the cytoplasm) is involved in many diverse cellular functions including controlling mitosis and DNA repair, cellular homeostasis, cell migration and/or cell proliferation. Balancing the cellular distribution of Pten is crucial to the function of the cell. Li and colleagues provide evidence that sorting of Pten to various organelles occurs in endosomes. Using bimolecular fluorescence complementation and dominant negative Rab5, they demonstrate that Rab5 and the E3 ligase adaptor protein Ndfip1 work together in to ubiquitinate Pten, which is required for its trafficking to the nucleus.