The Editorial Board of Molecular Biology of the Cell has highlighted the following articles from the February and March 2016 issues. From among the many fine articles in the journal, the Board selects for these Highlights articles that are of broad interest and significantly advance knowledge or provide new concepts or approaches that extend our understanding.
APC binds the Miro/Milton motor complex to stimulate transport of mitochondria to the plasma membrane
Kate M. Mills, Mariana G. Brocardo, and Beric R. Henderson
The role of adenomatous polyposis coli (APC) tumor suppressor at mitochondria is unclear. We show that APC associates with the Miro/Milton/kinesin complex to stimulate anterograde transport of mitochondria. This identifies the first regulatory role of APC in organelle transport. APC cancer mutations block this activity.
Mol. Biol. Cell 27 (3), 466–482
The alternate AP-1 adaptor subunit Apm2 interacts with the Mil1 regulatory protein and confers differential cargo sorting
Shawn T. Whitfield, Helen E. Burston, Björn D. M. Bean, Nandini Raghuram, Lymarie Maldonado-Báez, Michael Davey, Beverly Wendland, and Elizabeth Conibear
Adaptor complexes are important for cargo sorting in clathrin-coated vesicles. The µ adaptor subunits Apm1 and Apm2 create functionally distinct versions of the yeast AP-1 complex. A novel regulatory protein is identified that selectively binds Apm2-containing complexes and contributes to their membrane recruitment.
Mol. Biol. Cell 27 (3), 588–598
The casein kinases Yck1p and Yck2p act in the secretory pathway, in part, by regulating the Rab exchange factor Sec2p
Danièle Stalder and Peter J. Novick
Sec2p is phosphorylated by the redundant casein kinases Yck1p and Yck2p. This promotes the interaction of Sec2p with the downstream effector, Sec15p, and contributes to Sec2p localization and function. Phosphorylation requires prior association of Sec2p with vesicles and reduction of the inhibitory Golgi lipid PI(4)P from the vesicle membrane.
Mol. Biol. Cell 27 (4), 686–701
Functional analysis of the interface between the tandem C2 domains of synaptotagmin-1
Chantell S. Evans, Zixuan He, Hua Bai, Xiaochu Lou, Pia Jeggle, R. Bryan Sutton, J. Michael Edwardson, and Edwin R. Chapman
Synaptotagmin (syt)-1 is a Ca2+ sensor that triggers rapid synaptic vesicle exocytosis. Mutations that disrupt physical interactions between the tandem Ca2+-sensing modules (C2 domains) of syt-1 disrupt regulated membrane fusion in reconstituted fusion reactions and in neurons. Hence contacts between these domains are important for function.
Mol. Biol. Cell 27 (6), 979–989
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