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PDBsum entry 2kqs
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Transcription, apoptosis
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PDB id
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2kqs
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References listed in PDB file
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Key reference
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Title
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Structural and functional roles of daxx sim phosphorylation in sumo paralog-Selective binding and apoptosis modulation.
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Authors
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C.C.Chang,
M.T.Naik,
Y.S.Huang,
J.C.Jeng,
P.H.Liao,
H.Y.Kuo,
C.C.Ho,
Y.L.Hsieh,
C.H.Lin,
N.J.Huang,
N.M.Naik,
C.C.Kung,
S.Y.Lin,
R.H.Chen,
K.S.Chang,
T.H.Huang,
H.M.Shih.
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Ref.
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Mol Cell, 2011,
42,
62-74.
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PubMed id
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Abstract
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Small ubiquitin-like modifier (SUMO) conjugation and interaction are
increasingly associated with various cellular processes. However, little is
known about the cellular signaling mechanisms that regulate proteins for
distinct SUMO paralog conjugation and interactions. Using the transcriptional
coregulator Daxx as a model, we show that SUMO paralog-selective binding and
conjugation are regulated by phosphorylation of the Daxx SUMO-interacting motif
(SIM). NMR structural studies show that Daxx (732)E-I-I-V-L-S-D-S-D(740) is a
bona fide SIM that binds to SUMO-1 in a parallel orientation. Daxx-SIM is
phosphorylated by CK2 kinase at residues S737 and S739. Phosphorylation promotes
Daxx-SIM binding affinity toward SUMO-1 over SUMO-2/3, causing Daxx preference
for SUMO-1 conjugation and interaction with SUMO-1-modified factors.
Furthermore, Daxx-SIM phosphorylation enhances Daxx to sensitize stress-induced
cell apoptosis via antiapoptotic gene repression. Our findings provide
structural insights into the Daxx-SIM:SUMO-1 complex, a model of SIM
phosphorylation-enhanced SUMO paralog-selective modification and interaction,
and phosphorylation-regulated Daxx function in apoptosis.
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