TY - JOUR
T1 - Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins
AU - Wood, Jonathan D.
AU - Yuan, Joseph
AU - Margolis, Russell L.
AU - Colomer, Veronica
AU - Duan, Kui
AU - Kushi, Jonathan
AU - Kaminsky, Zachary
AU - Kleiderlein, John J.
AU - Sharp, Alan H.
AU - Ross, Christopher A.
N1 - Funding Information:
This work was supported by NIH Grants NS16375, NS34172, and MH01275-01A1 and an MRC (UK) traveling fellowship to J.D.W. We are grateful to Anthony Lanahan for the human fetal brain library in pPC86, Roxann Ashworth for assistance with DNA sequencing, and Peter Faber for the pGEX-HYPA construct.
PY - 1998/6
Y1 - 1998/6
N2 - Atrophin-1 contains a polyglutamine repeat, expansion of which is responsible for dentatorubral and pallidoluysian atrophy (DRPLA). The normal function of atrophin-1 is unknown. We have identified five atrophin-1 interacting proteins (AIPs) which bind to atrophin-1 in the vicinity of the polyglutamine tract using the yeast two-hybrid system. Four of the interactions were confirmed using in vitro binding assays. All five interactors contained multiple WW domains. Two are novel. The AlPs can be divided into two distinct classes. AIP1 and AIP3/WWP3 are MAGUK-like multidomain proteins containing a number of protein-protein interaction modules, namely a guanylate kinase-like region, two WW domains, and multiple PDZ domains. AIP2/WWP2, ALP4, and AIP5/WWP1 are highly homologous, each having four WW domains and a HECT domain characteristic of ubiquitin ligases. These interactors are similar to recently isolated huntingtin-interacting proteins, suggesting possible commonality of function between two proteins responsible for very similar diseases.
AB - Atrophin-1 contains a polyglutamine repeat, expansion of which is responsible for dentatorubral and pallidoluysian atrophy (DRPLA). The normal function of atrophin-1 is unknown. We have identified five atrophin-1 interacting proteins (AIPs) which bind to atrophin-1 in the vicinity of the polyglutamine tract using the yeast two-hybrid system. Four of the interactions were confirmed using in vitro binding assays. All five interactors contained multiple WW domains. Two are novel. The AlPs can be divided into two distinct classes. AIP1 and AIP3/WWP3 are MAGUK-like multidomain proteins containing a number of protein-protein interaction modules, namely a guanylate kinase-like region, two WW domains, and multiple PDZ domains. AIP2/WWP2, ALP4, and AIP5/WWP1 are highly homologous, each having four WW domains and a HECT domain characteristic of ubiquitin ligases. These interactors are similar to recently isolated huntingtin-interacting proteins, suggesting possible commonality of function between two proteins responsible for very similar diseases.
UR - http://www.scopus.com/inward/record.url?scp=0031807249&partnerID=8YFLogxK
U2 - 10.1006/mcne.1998.0677
DO - 10.1006/mcne.1998.0677
M3 - Article
C2 - 9647693
AN - SCOPUS:0031807249
SN - 1044-7431
VL - 11
SP - 149
EP - 160
JO - Molecular and Cellular Neuroscience
JF - Molecular and Cellular Neuroscience
IS - 3
ER -