PDBsum entry 2kqs

Transcription, apoptosis

PDB id: 2kqs

Contents

Protein chains

97 a.a. *

20 a.a. *

* Residue conservation analysis

PDB id:

2kqs

Name:

Transcription, apoptosis

Title:

Phosphorylation of sumo-interacting motif by ck2 enhances daxx sumo binding activity

Structure:

Small ubiquitin-related modifier 1. Chain: a. Synonym: sumo-1, sentrin, ubiquitin-like protein smt3c, smt3 homolog 3, ubiquitin-homology domain protein pic1, ubiquitin-like protein ubl1, gap-modifying protein 1, gmp1. Engineered: yes. Death domain-associated protein 6. Chain: b. Fragment: unp residues 721-741.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ok/sw-cl.43, smt3c, smt3h3, sumo1, ubl1. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: the peptide was chemically synthesized. The sequence of the peptide is naturally found in homo sapiens (human)

NMR struc:

20 models

Authors:

M.T.Naik,T.H.Huang,H.Shih

Key ref:

C.C.Chang et al. (2011). Structural and functional roles of Daxx SIM phosphorylation in SUMO paralog-selective binding and apoptosis modulation. Mol Cell, 42, 62-74. PubMed id: 21474068

Date:

17-Nov-09 Release date: 01-Dec-10

Protein chain

P63165  (SUMO1_HUMAN) -  Small ubiquitin-related modifier 1 from Homo sapiens

Seq: 101 a.a.

Struc: 97 a.a.

Protein chain

Q9UER7  (DAXX_HUMAN) -  Death domain-associated protein 6 from Homo sapiens

Seq: 740 a.a.

Struc: 20 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

Mol Cell 42:62-74 (2011)

PubMed id: 21474068

Structural and functional roles of Daxx SIM phosphorylation in SUMO paralog-selective binding and apoptosis modulation.

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.

ABSTRACT

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.