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Accepted Articles (Accepted, unedited articles published online and citable. The final edited and typeset version of record will appear in future.)

Edited By: Michael S. Marks, Mark C. P. Marsh, Trina A. Schroer, Tom H. Stevens

Online ISSN: 1600-0854

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  1. Original Articles

    1. Rab12 localizes to Shiga toxin-induced plasma membrane invaginations and controls toxin transport

      Gustaf E. Rydell, Henri-François Renard, Maria-Daniela Garcia-Castillo, Florent Dingli, Damarys Loew, Christophe Lamaze, Winfried Römer and Ludger Johannes

      Accepted manuscript online: 4 APR 2014 08:57AM EST | DOI: 10.1111/tra.12173

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      Synopsis

      SILAC labeling and quantitative mass spectrometry were used to identify Rab12 on Shiga toxin-induced endocytic plasma membrane invaginations. Localization of GFP-Rab12 on these structures was shown by fluorescence microscopy. Shiga toxin trafficking to trans-Golgi/TGN membranes and toxin-mediated inhibition of protein biosynthesis were inhibited in Rab12-depleted cells, suggesting that Rab12 functions in the retrograde transport route.

    2. Role of adaptor proteins and clathrin in the trafficking of human kidney anion exchanger 1 (kAE1) to the cell surface

      Mutita Junking, Nunghathai Sawasdee, Natapol Duangtum, Boonyarit Cheunsuchon, Thawornchai Limjindaporn and Pa-thai Yenchitsomanus

      Accepted manuscript online: 3 APR 2014 12:41PM EST | DOI: 10.1111/tra.12172

      Thumbnail image of graphical abstract

      Synopsis

      Mutations of SLC4A1 encoding kidney anion exchanger 1 (kAE1) result in distal renal tubular acidosis (dRTA). The mutant kAE1 shows basolateral trafficking defect in α-intercalated cells. It is not clear how the normal intracellular trafficking of kAE1 occurs. We identified the proteins involved in intracellular sorting and trafficking of kAE1 in kidney cell lines and human kidney tissues. Adaptor protein complexes (AP-1 mu1A, AP-3 mu1, and AP-4 mu1) and clathrin play crucial role in intracellular sorting and trafficking of human kAE1

    3. A biophysical analysis of mitochondrial movement: differences between transport in neuronal cell bodies versus processes

      Babu Reddy Janakaloti Narayanareddy, Suvi Vartiainen, Neema Hariri, Diane K. O'Dowd and Steven P. Gross

      Accepted manuscript online: 27 MAR 2014 08:39PM EST | DOI: 10.1111/tra.12171

      Thumbnail image of graphical abstract

      Synopsis

      Is cargo transport affected by subcellular location? We quantify motion of different size mitochondria in neuronal cell bodies and processes, and discover that movement is different in these two regions. In cell bodies, mitochondria move relatively rapidly, and motion is size-independent. In contrast, both velocity and run distances are decreased in processes, and are inversely correlated with mitochondrial size. Decreasing confinement via hypotonic treatment improved transport in the processes, but not the cell body. Our data thus suggests that motor mediated transport is significantly impeded in the more confined environment of the processes.

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