CHC22 is needed for retrograde trafficking from endosomes to the trans-Golgi, unlike its clathrin sibling CHC17, and in a manner distinct from retromer

Acton

Antonescu

Arighi

Banting

Benmerah

Bennett

Bolte

Borner

Brodsky

Brüning

Bujny

Chen

Chih-Ying Chen

Christopher Esk

Dell’Angelica

Fazakerley

Frances M. Brodsky

Frittoli

Ganley

Garvey

Hehnly

Hinrichsen

Hood

Huang

Johannes

Karylowski

Kedra

Kerr

Lombardi

Ludger Johannes

Maianu

Mallard

Mardones

Meyer

Michael

Motley

Nokes

Popoff

Riederer

Rojas

Saint-Pol

Seaman

Shepherd

Shewan

Sirotkin

Tang

Towler

Ungewickell

van Steensel

Vassilopoulos

Wainszelbaum

Wakeham

Wassmer

Williams

Wong

English

PubMed

Crossref

The clathrin heavy chain isoform CHC22 functions in a novel endosomal sorting step

Clathrin heavy chain 22 (CHC22) is an isoform of the well-characterized CHC17 clathrin heavy chain, a coat component of vesicles that mediate endocytosis and organelle biogenesis. CHC22 has a distinct role from CHC17 in trafficking glucose transporter 4 (GLUT4) in skeletal muscle and fat, though its transfection into HEK293 cells suggests functional redundancy. Here, we show that CHC22 is eightfold less abundant than CHC17 in muscle, other cell types have variably lower amounts of CHC22, and endogenous CHC22 and CHC17 function independently in nonmuscle and muscle cells. CHC22 was required for retrograde trafficking of certain cargo molecules from endosomes to the trans-Golgi network (TGN), defining a novel endosomal-sorting step distinguishable from that mediated by CHC17 and retromer. In muscle cells, depletion of syntaxin 10 as well as CHC22 affected GLUT4 targeting, establishing retrograde endosome-TGN transport as critical for GLUT4 trafficking. Like CHC22, syntaxin 10 is not expressed in mice but is present in humans and other vertebrates, implicating two species-restricted endosomal traffic proteins in GLUT4 transport

Esk, Christopher

Chen, Chih-Ying

Johannes, Ludger

Brodsky, Frances M

eScholarship - University of California

A guided tour into subcellular colocalization analysis in light microscopy.

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Comparative proteomics of clathrin-coated vesicles.

Early/recycling endosomesto-TGN transport involves two SNARE complexes and a Rab6 isoform.

Imaging was performed at room temperature using Nikon immersion oil and Leica Type F immersion oil. DAPI, Alexa 488, Alexa 555, Alexa 568, Alexa 647, and TO-PRO3 fluorescence was sequentially excited using lasers with wavelengths of 405 (DAPI),

The trans-Golgi network accessory protein p56 promotes long-range movement of GGA/clathrin-containing transport carriers and lysosomal enzyme sorting.

http://jcb.rupress.org/content/jcb/188/1/131.full.pdf

The clathrin heavy chain isoform CHC22 functions in a novel endosomal sorting step

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