Cover image for Vol. 18 Issue 7

Edited By: Michael S. Marks, Trina A. Schroer, Robert G. Parton and Sharon A. Tooze

Online ISSN: 1600-0854

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Recently Published Articles

  1. The Arl3 and Arl1 GTPase cooperates with Cog8 to regulate selective autophagy via Atg9 trafficking

    I-Hao Wang, Yi-Jie Chen, Jia-Wei Hsu and Fang-Jen S. Lee

    Accepted manuscript online: 19 JUN 2017 06:40AM EST | DOI: 10.1111/tra.12498

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    Arf-like small GTPase had been reported to participate in different vesicle transport events. In this study, we demonstrate that Arl3-Arl1 small GTPase cascade cooperates with the subunit of COG complex to control Cvt pathway but not non-selective autophagy. The yeast strains with dysfunction of Arl3-Arl1 cascade and COG complex accumulate Atg9 at the late Golgi in nutrient-rich condition, thereby causing the defect of Cvt pathway. Thus, two Golgi-endosomal traffic components coordinately regulate the Cvt pathway by regulating Atg9 trafficking at the Golgi.

  2. The big and intricate dreams of little organelles: Embracing complexity in the study of membrane traffic

    Allen P. Liu, Roberto J. Botelho and Costin N. Antonescu

    Accepted manuscript online: 2 JUN 2017 05:08AM EST | DOI: 10.1111/tra.12497

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    Organelle dynamics and membrane traffic are integrated within complex, multiscale, and non-linear regulatory networks that impact virtually every aspect of cell physiology. In this review, we discuss systematic approaches that have revealed the complexity of these phenomena, and discuss molecular versatility and organelle heterogeneity, as well as organelle adaptation under specific cellular conditions. Organelle dynamics and membrane traffic are functionally heterogeneous and adaptable processes that coordinate with higher-order system behaviour to optimize cell function under a range of contexts.

  3. Enzyme reversal to explore the function of yeast E3 ubiquitin-ligases (pages 465–484)

    Chris MacDonald, Stanley Winistorfer, Robert M. Pope, Michael E. Wright and Robert C. Piper

    Version of Record online: 1 JUN 2017 | DOI: 10.1111/tra.12485

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    MacDonald et al describe a library of anti-ligase reagents that antagonize the activity of endogenous E3 ubiquitin ligases, perturbing their function and stabilizing endogenous substrate levels. The library was used to identify E3 ligases required for vacuolar sorting from the biosynthetic and endocytic pathways.

  4. Oxysterol-binding protein recruitment and activity at the endoplasmic reticulum-Golgi interface are independent of Sac1

    Mark Charman, Asako Goto and Neale D. Ridgway

    Version of Record online: 31 MAY 2017 | DOI: 10.1111/tra.12491

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    Phosphatidylinositol 4-phosphate (PI-4P) mediates oxysterol-binding protein (OSBP) recruitment at endoplasmic reticulum (ER)-Golgi membrane contact sites (MCS) as well as counter-current cholesterol transport. Like OSBP, the PI-4P phosphatase Sac1 localizes to the Golgi apparatus in response to cholesterol depletion, oxysterols and p38 inhibition, resulting in reduced Golgi PI-4P. However, Sac1 does not regulate OSBP recruitment to MCS or its ability to activate ceramide transfer protein (CERT) and sphingomyelin synthesis. OSBP utilizes a specific pool of PI-4P at the ER-Golgi interface that is independent of Sac1 activity.

  5. Syntaxin 4 mediates endosome recycling for lytic granule exocytosis in cytotoxic T-lymphocytes (pages 442–452)

    Waldo A. Spessott, Maria L. Sanmillan, Vineet V. Kulkarni, Margaret E. McCormick and Claudio G. Giraudo

    Version of Record online: 28 MAY 2017 | DOI: 10.1111/tra.12490

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    Destruction of transformed or infected cells by cytotoxic T-lymphocytes depends upon recycling of effector proteins through Rab11a endosomes. However, little is known about SNAREs mediating this trafficking step. Here, we establish that syntaxin 4 (STX4) is necessary for Rab11a endosome fusion at the immunological synapse, which in turn is required for normal fusion of lytic granules and therefore for T-lymphocyte cytolytic activity. Our data reveal the importance of STX4 in cytotoxic immune responses, a key process for adaptive immunity.