ESCRT-III has an escort

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ESCRT-III has an escort

jcb.201007018”> Wemmer et al. show. Like a big brother, Bro1 protects a protein complex that helps pinch off vesicles. The ESCRT-III complex serves as a pair of molecular scissors that cuts cell membranes, helping to separate dividing cells and enabling viruses such as HIV to bud from the cell surface. The complex also helps endosomes fashion intralumenal vesicles (ILVs), which hold wo...

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ESCRT-III gets the bends

Mitotic cells’ shocking response to stress E lsing et al. reveal how some vulnerable mitotic cells protect themselves from stress. One way that cells cope with stress is by making heat-shock proteins such as Hsp70 that shield other proteins from damage. The transcription factor HSF1 serves as the main activator for heat-shock protein genes. During interphase, another transcription factor, HSF2,...

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Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly.

The AAA+ ATPase VPS4 plays an essential role in multivesicular body biogenesis and is thought to act by disassembling ESCRT-III complexes. VPS4 oligomerization and ATPase activity are promoted by binding to LIP5. LIP5 also binds to the ESCRT-III like protein CHMP5/hVps60, but how this affects its function remains unclear. Here we confirm that LIP5 binds tightly to CHMP5, but also find that it b...

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Comparative analysis of ESCRT-I, ESCRT-II and ESCRT-III function in Drosophila by efficient isolation of ESCRT mutants.

ESCRT proteins were initially isolated in yeast as a single functional set of conserved components controlling endosomal cargo sorting and multivesicular body (MVB) biogenesis. Recent work has suggested that metazoan ESCRT proteins might have more functionally diverse roles, but the limited availability of ESCRT mutants in species other than yeast has hampered a thorough analysis. Here, we used...

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ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes.

The endosomal sorting complexes required for transport (ESCRT) proteins have a critical function in abscission, the final separation of the daughter cells during cytokinesis. Here, we describe the structure and function of a previously uncharacterized ESCRT-III interacting protein, MIT-domain containing protein 1 (MITD1). Crystal structures of MITD1 reveal a dimer, with a microtubule-interactin...

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ژورنال

عنوان ژورنال: Journal of Cell Biology

سال: 2011

ISSN: 1540-8140,0021-9525

DOI: 10.1083/jcb.1922iti1