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Title
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Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins.
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Authors
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J.D.Wood,
J.Yuan,
R.L.Margolis,
V.Colomer,
K.Duan,
J.Kushi,
Z.Kaminsky,
J.J.Kleiderlein,
A.H.Sharp,
C.A.Ross.
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Ref.
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Mol Cell Neurosci, 1998,
11,
149-160.
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PubMed id
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Abstract
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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 AIPs 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, AIP4, 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.
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