HIP1 and HIP12 Display Differential Binding to F-actin, AP2, and Clathrin
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چکیده
منابع مشابه
HIP1 functions in clathrin-mediated endocytosis through binding to clathrin and adaptor protein 2.
Polyglutamine expansion in huntingtin is the underlying mutation leading to neurodegeneration in Huntington disease. This mutation influences the interaction of huntingtin with different proteins, including huntingtin-interacting protein 1 (HIP1), in which affinity to bind to mutant huntingtin is profoundly reduced. Here we demonstrate that HIP1 colocalizes with markers of clathrin-mediated end...
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The interaction between HIP family proteins (HIP1 and HIP12/1R) and clathrin is fundamental to endocytosis. We used circular dichroism (CD) to study the stability of an HIP1 subfragment (aa468-530) that is splayed open. CD thermal melts show HIP1 468-530 is only stable at low temperatures, but this HIP1 fragment contains a structural unit that does not melt out even at 83°C. We then created HIP...
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15 صفحه اولBinding of myosin A to F-actin.
The studies of Szent-Gyorgyi (1) have clearly established the formation of actomyosin from F-actin and myosin A. SzentGyorgyi (l), Portzehl, Schramm, and Weber (2), Jaisle (3), Snellman and Gelotte (4), and Spicer and Gergely (5) have suggested from their viscometric and centrifugal studies that the maximal amount of myosin A which can be bound by F-actin is in the ratio of 2 to 4 : 1, by weigh...
متن کاملAdenosine Triphosphate Cleavage during the G-actin to F-actin Transformation and the Binding of Adenosine Diphosphate to F-actin.
Since the discovery by Straub and Feuer (1) and by Laki, Bowen, and Clark (2) that adenosine triphosphate bound to Gactin is transformed to adenosine diphosphate and inorganic phosphate during polymerization of actin, it has become increasingly clear that the chemical changes in the nucleotide are related to the change in the physical state of the protein. Barany, 13iro, Molnar, and Straub have...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2002
ISSN: 0021-9258
DOI: 10.1074/jbc.m112310200