scholarly journals Clathrin binding to the DLLRKN region of Huntingtin‐interacting protein 1 (HIP1) requires coiled coil instability

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Joel Alcasid Ybe ◽  
Arun Alphonse Ignatius ◽  
David Giedroc ◽  
Melissa Illingworth ◽  
Sara Poorfarahani
2010 ◽  
Vol 66 (3) ◽  
pp. 314-318 ◽  
Author(s):  
Jeremy D. Wilbur ◽  
Peter K. Hwang ◽  
Frances M. Brodsky ◽  
Robert J. Fletterick

Huntingtin-interacting protein 1 (HIP1) is an important link between the actin cytoskeleton and clathrin-mediated endocytosis machinery. HIP1 has also been implicated in the pathogenesis of Huntington's disease. The binding of HIP1 to actin is regulated through an interaction with clathrin light chain. Clathrin light chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding. To understand the mechanism of this conformational regulation, a high-resolution crystal structure of a stable fragment from the HIP1 coiled-coil domain was determined. The flexibility of the HIP1 coiled-coil region was evident from its variation from a previously determined structure of a similar region. A hydrogen-bond network and changes in coiled-coil monomer interaction suggest that the HIP1 coiled-coil domain is uniquely suited to allow conformational flexibility.


2005 ◽  
Vol 170 (2) ◽  
pp. 191-200 ◽  
Author(s):  
Ian G. Mills ◽  
Luke Gaughan ◽  
Craig Robson ◽  
Theodora Ross ◽  
Stuart McCracken ◽  
...  

Internalization of activated receptors regulates signaling, and endocytic adaptor proteins are well-characterized in clathrin-mediated uptake. One of these adaptor proteins, huntingtin interacting protein 1 (HIP1), induces cellular transformation and is overexpressed in some prostate cancers. We have discovered that HIP1 associates with the androgen receptor through a central coiled coil domain and is recruited to DNA response elements upon androgen stimulation. HIP1 is a novel androgen receptor regulator, significantly repressing transcription when knocked down using a silencing RNA approach and activating transcription when overexpressed. We have also identified a functional nuclear localization signal at the COOH terminus of HIP1, which contributes to the nuclear translocation of the protein. In conclusion, we have discovered that HIP1 is a nucleocytoplasmic protein capable of associating with membranes and DNA response elements and regulating transcription.


2000 ◽  
Vol 275 (52) ◽  
pp. 41299-41308 ◽  
Author(s):  
Abigail S. Hackam ◽  
Ayman S. Yassa ◽  
Roshni Singaraja ◽  
Martina Metzler ◽  
Claire-Anne Gutekunst ◽  
...  

2007 ◽  
Vol 67 (18) ◽  
pp. 8923-8931 ◽  
Author(s):  
Sarah V. Bradley ◽  
Mitchell R. Smith ◽  
Teresa S. Hyun ◽  
Peter C. Lucas ◽  
Lina Li ◽  
...  

2008 ◽  
Vol 28 (3) ◽  
pp. 599-609 ◽  
Author(s):  
Justin N. Moores ◽  
Sophie Roy ◽  
Donald W. Nicholson ◽  
Brian E. Staveley

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