scholarly journals Crystal Structure at 2.8 Å of Huntingtin-Interacting Protein 1 (HIP1) Coiled-Coil Domain Reveals a Charged Surface Suitable for HIP1 Protein Interactor (HIPPI)

2008 ◽  
Vol 375 (5) ◽  
pp. 1197-1205 ◽  
Author(s):  
Qian Niu ◽  
Joel A. Ybe
Keyword(s):  
Crystal Structure ◽  
Coiled Coil ◽  
Charged Surface ◽  
Interacting Protein ◽  
Coiled Coil Domain ◽  
Huntingtin Interacting Protein 1 ◽  
Huntingtin Interacting Protein

scholarly journals Accommodation of structural rearrangements in the huntingtin-interacting protein 1 coiled-coil domain

2010 ◽  
Vol 66 (3) ◽  
pp. 314-318 ◽  
Author(s):  
Jeremy D. Wilbur ◽  
Peter K. Hwang ◽  
Frances M. Brodsky ◽  
Robert J. Fletterick
Keyword(s):  
Light Chain ◽  
Coiled Coil ◽  
Actin Binding ◽  
Interacting Protein ◽  
Similar Region ◽  
Coiled Coil Domain ◽  
Coiled Coil Region ◽  
Huntingtin Interacting Protein 1 ◽  
Conformational Regulation ◽  
Huntingtin Interacting Protein

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.

scholarly journals Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors

2005 ◽  
Vol 170 (2) ◽  
pp. 191-200 ◽  
Author(s):  
Ian G. Mills ◽  
Luke Gaughan ◽  
Craig Robson ◽  
Theodora Ross ◽  
Stuart McCracken ◽  
...  
Keyword(s):  
Androgen Receptor ◽  
Hormone Receptors ◽  
Nuclear Translocation ◽  
Coiled Coil ◽  
Adaptor Proteins ◽  
Cellular Transformation ◽  
Interacting Protein ◽  
Response Elements ◽  
Huntingtin Interacting Protein 1 ◽  
Huntingtin Interacting Protein

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.

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
Keyword(s):  
Coiled Coil ◽  
Interacting Protein ◽  
Huntingtin Interacting Protein 1 ◽  
Huntingtin Interacting Protein

HZwint-1, a novel human kinetochore component that interacts with HZW10

2000 ◽  
Vol 113 (11) ◽  
pp. 1939-1950 ◽  
Author(s):  
D.A. Starr ◽  
R. Saffery ◽  
Z. Li ◽  
A.E. Simpson ◽  
K.H. Choo ◽  
...  
Keyword(s):  
Hela Cells ◽  
Coiled Coil ◽  
Yeast Two Hybrid ◽  
Interacting Protein ◽  
Dicentric Chromosomes ◽  
Centromere Function ◽  
Coiled Coil Domain ◽  
Gfp Fluorescence ◽  
Two Hybrid ◽  
Active Centromere

HZwint-1 (Human ZW10 interacting protein-1) was identified in a yeast two hybrid screen for proteins that interact with HZW10. HZwint-1 cDNA encodes a 43 kDa protein predicted to contain an extended coiled-coil domain. Immunofluorescence studies with sera raised against HZwint-1 protein revealed strong kinetochore staining in nocodazole-arrested chromosome spreads. This signal co-localizes at the kinetochore with HZW10, at a position slightly outside of the central part of the centromere as revealed by staining with a CREST serum. The kinetochore localization of HZwint-1 has been confirmed by following GFP fluorescence in HeLa cells transiently transfected with a plasmid encoding a GFP/HZwint-1 fusion protein. In cycling HeLa cells, HZwint-1 localizes to the kinetochore of prophase HeLa cells prior to HZW10 localization, and remains at the kinetochore until late in anaphase. This localization pattern, combined with the two-hybrid results, suggests that HZwint-1 may play a role in targeting HZW10 to the kinetochore at prometaphase. HZwint-1 was also found to localize to neocentromeres and to the active centromere of dicentric chromosomes. HZwint-1 thus appears to associate with all active centromeres, implying that it plays an important role in correct centromere function.

scholarly journals Huntingtin Interacting Protein 1 Induces Apoptosis via a Novel Caspase-dependent Death Effector Domain

2000 ◽  
Vol 275 (52) ◽  
pp. 41299-41308 ◽  
Author(s):  
Abigail S. Hackam ◽  
Ayman S. Yassa ◽  
Roshni Singaraja ◽  
Martina Metzler ◽  
Claire-Anne Gutekunst ◽  
...  
Keyword(s):  
Interacting Protein ◽  
Effector Domain ◽  
Death Effector Domain ◽  
Huntingtin Interacting Protein 1 ◽  
Death Effector ◽  
Huntingtin Interacting Protein
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