scholarly journals Increased Expression of the Huntingtin Interacting Protein-1 Gene in Cells From Hutchinson Gilford Syndrome (Progeria) Patients and Aged Donors

2003 ◽  
Vol 58 (10) ◽  
pp. B873-B878 ◽  
Author(s):  
S. Chigira ◽  
K. Sugita ◽  
K. Kita ◽  
S. Sugaya ◽  
Y. Arase ◽  
...  
Keyword(s):  
Interacting Protein ◽  
Huntingtin Interacting Protein 1 ◽  
Huntingtin Interacting Protein ◽  
In Cells

scholarly journals The Huntingtin-interacting protein SETD2/HYPB is an actin lysine methyltransferase

2020 ◽  
Vol 6 (40) ◽  
pp. eabb7854 ◽  
Author(s):  
Riyad N. H. Seervai ◽  
Rahul K. Jangid ◽  
Menuka Karki ◽  
Durga Nand Tripathi ◽  
Sung Yun Jung ◽  
...  
Keyword(s):  
Cell Migration ◽  
Actin Filaments ◽  
Actin Polymerization ◽  
Scaffolding Protein ◽  
Actin Binding ◽  
Set Domain ◽  
Interacting Protein ◽  
Lysine Methyltransferase ◽  
Huntingtin Interacting Protein ◽  
In Cells

The methyltransferase SET domain–containing 2 (SETD2) was originally identified as Huntingtin (HTT) yeast partner B. However, a SETD2 function associated with the HTT scaffolding protein has not been elucidated, and no linkage between HTT and methylation has yet been uncovered. Here, we show that SETD2 is an actin methyltransferase that trimethylates lysine-68 (ActK68me3) in cells via its interaction with HTT and the actin-binding adapter HIP1R. ActK68me3 localizes primarily to the insoluble F-actin cytoskeleton in cells and regulates actin polymerization/depolymerization dynamics. Disruption of the SETD2-HTT-HIP1R axis inhibits actin methylation, causes defects in actin polymerization, and impairs cell migration. Together, these data identify SETD2 as a previously unknown HTT effector regulating methylation and polymerization of actin filaments and provide new avenues for understanding how defects in SETD2 and HTT drive disease via aberrant cytoskeletal methylation.

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

scholarly journals Aberrant Huntingtin Interacting Protein 1 in Lymphoid Malignancies

2007 ◽  
Vol 67 (18) ◽  
pp. 8923-8931 ◽  
Author(s):  
Sarah V. Bradley ◽  
Mitchell R. Smith ◽  
Teresa S. Hyun ◽  
Peter C. Lucas ◽  
Lina Li ◽  
...  
Keyword(s):  
Interacting Protein ◽  
Lymphoid Malignancies ◽  
Huntingtin Interacting Protein 1 ◽  
Huntingtin Interacting Protein

Huntingtin interacting protein 1 can regulate neurogenesis inDrosophila

2008 ◽  
Vol 28 (3) ◽  
pp. 599-609 ◽  
Author(s):  
Justin N. Moores ◽  
Sophie Roy ◽  
Donald W. Nicholson ◽  
Brian E. Staveley
Keyword(s):  
Interacting Protein ◽  
Huntingtin Interacting Protein 1 ◽  
Huntingtin Interacting Protein

scholarly journals It's HIP to be a hub

2005 ◽  
Vol 170 (2) ◽  
pp. 169-171 ◽  
Author(s):  
Manuela Vecchi ◽  
Pier Paolo Di Fiore
Keyword(s):  
Network Theory ◽  
Transcriptional Activity ◽  
Hormone Receptors ◽  
Nuclear Hormone Receptors ◽  
Interacting Protein ◽  
Endocytic Protein ◽  
Huntingtin Interacting Protein 1 ◽  
Huntingtin Interacting Protein ◽  
Endocytic Proteins

Many endocytic proteins shuttle between the nucleus and the cytoplasm; however, their putative function in the nucleus is unclear. Now, new data demonstrate that huntingtin interacting protein 1 (HIP1), an endocytic protein, modulates the transcriptional activity of nuclear hormone receptors. In network theory, therefore, HIP1 can be regarded as a hub connecting heterogeneous functional “territories:” a possibility with important physiological and pathological implications.

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