Active Arf6 Recruits ARNO/Cytohesin GEFs to the PM by Binding Their PH Domains
نویسندگان
چکیده
منابع مشابه
Adenovirus Recruits Dynein by an Evolutionary Novel Mechanism Involving Direct Binding to pH-Primed Hexon
Following receptor-mediated uptake into endocytic vesicles and escape from the endosome, adenovirus is transported by cytoplasmic dynein along microtubules to the perinuclear region of the cell. How motor proteins are recruited to viruses for their own use has begun to be investigated only recently. We review here the evidence for a role for dynein and other motor proteins in adenovirus infecti...
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Pleckstrin homology (PH) domains share low sequence identities but extremely conserved structures. They have been found in many proteins for cellular signal-dependent membrane targeting by binding inositol phosphates to perform different physiological functions. In order to understand the sequence-structure relationship and binding specificities of PH domains, quantum mechanical (QM) calculatio...
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The ADP-ribosylation factors (Arfs) are a family of Rasrelated, low molecular mass ( 20 kDa), GTP-binding proteins that are expressed in all eukaryotes. There are six mammalian Arfs and many more Arf-like proteins. Like all GTPases, Arfs cycle between GDP-bound, inactive and GTP-bound, active states. In the active state, Arfs interact with proteins and other effector molecules to carry out thei...
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ژورنال
عنوان ژورنال: Molecular Biology of the Cell
سال: 2007
ISSN: 1059-1524,1939-4586
DOI: 10.1091/mbc.e06-11-0998