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Cover image for Vol. 18 Issue 12

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

Online ISSN: 1600-0854

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Advances in Cell Biology in China

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Celebrating the Contributions of Ari Helenius

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Chemical and Immunological Synapses"

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Recently Published Articles

  1. Distinct features of multivesicular body-lysosome fusion revealed by a new cell-free content-mixing assay

    Mahmoud Abdul Karim, Dieter Ronny Samyn, Sevan Mattie and Christopher Leonard Brett

    Version of Record online: 10 DEC 2017 | DOI: 10.1111/tra.12543

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    Endocytosis culminates with multivesicular bodies (MVBs) fusing with lysosomes. But the molecular underpinnings of this event remain unclear. Here, using Saccharomyces cerevisiae as a model, Karim et al employ a new in vitro assay to show that MVB-lysosome fusion is driven by endosomal sorting complexes required for transport (ESCRT)-dependent Rab-GTPase activation and the syntaxin ortholog Pep12, distinguishing it from other lysosome membrane fusion events.

  2. Deciphering lipid codes: K-Ras as a paradigm

    Yong Zhou and John F. Hancock

    Version of Record online: 10 DEC 2017 | DOI: 10.1111/tra.12541

    Thumbnail image of graphical abstract

    Plasma membrane (PM) is a highly heterogeneous environment and contains various nano-domains with distinct local lipid composition. Lipid-anchored small GTPases Ras proteins use their C-terminal membrane anchoring features for specific lipid sorting. In particular, K-Ras has a C-terminal hexa-lysine polybasic domain and an adjacent farnesyl anchor, which together allow the capability to selectively sort acidic phosphatidylserine lipids in the inner leaflet of the PM. This summarizes the latest findings in K-Ras-selective lipid sorting and the potential biological implications.

  3. TMD1 domain and CRAC motif determine the association and disassociation of MxIRT1 with detergent-resistant membranes

    Song Tan, Peng Zhang, Wei Xiao, Bing Feng, Lan-You Chen, Shuang Li, Peng Li, Wei-Zhong Zhao, Xiao-Ting Qi and Li-Ping Yin

    Version of Record online: 5 DEC 2017 | DOI: 10.1111/tra.12540

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    Malus xiaojinesis IRT1 (MxIRT1) is a plasma membrane (PM)-localized Fe2+ transporter. We found that MxIRT1 PM targeting and function depend on the association with detergent-resistant membranes (DRMs, a biochemical counterpart of PM microdomains). This association occurs in endoplasmic reticulum (ER), and it is determined by transmembrane domain 1 (TMD1) of MxIRT1. After intracellular traffic and exocytosis into PM via vesicle, cholesterol recognition/interaction amino acid consensus (CRAC) motif of MxIRT1 regulates the shift of MxIRT1 from PM microdomains to PM homogeneous regions, and thus activates MxIRT1-mediated Fe2+ uptake.

  4. Tau directs intracellular trafficking by regulating the forces exerted by kinesin and dynein teams

    Abdullah R. Chaudhary, Florian Berger, Christopher L. Berger and Adam G. Hendricks

    Version of Record online: 5 DEC 2017 | DOI: 10.1111/tra.12537

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    We isolated endogenous cargoes, along with a complement of kinesin-1, kinesin-2, and dynein motors, and reconstituted their bidirectional motility in vitro. We find that tau, a microtubule-associated protein that stabilizes microtubules in neuronal axons, directs bidirectional cargoes towards the microtubule minus end by tuning the balance of forces exerted by kinesin and dynein teams. These results suggest a general mechanism for regulating the transport of intracellular cargoes through modulating the relative activity of opposing motor teams.

  5. You have full text access to this OnlineOpen article
    The biology and polymer physics underlying large-scale chromosome organization

    Shelley Sazer and Helmut Schiessel

    Version of Record online: 3 DEC 2017 | DOI: 10.1111/tra.12539

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    Deciphering the basic principles of chromosome organization from the separate perspectives of biology and polymer physics has undergone paradigm shifts over many decades, but these 2 fields have now converged on a model that explains the formation and positioning of loops and the loopy globule organization of chromosomes in interphase eukaryotic cells. According to this model, the cohesin complex binds to DNA and extrudes a loop of DNA until it reaches CTCF proteins bound to convergently positioned binding sites.

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