Backbone 1H, 13C, and 15N assignments for the tandem ubiquitin binding domains of signal transducing adapter molecule 1

Title
Backbone 1H, 13C, and 15N assignments for the tandem ubiquitin binding domains of signal transducing adapter molecule 1
Authors
임종수홍윤헌이봉진안희철
Keywords
STAM; ESCRT; NMR; ubiquitin; Signal transducing adapter molecule; Vps27/Hrs/Stam (VHS); interacting motif (UIM); Poly-ubiquitin; Backbone resonance assignments
Issue Date
2011-04
Publisher
BIOMOLECULAR NMR ASSIGNMENTS
Citation
VOL 5, NO 1, 51-54
Abstract
Signal transducing adapter molecule (STAM) forms the endosomal sorting complex required for transport- 0 (ESCRT-0) complex with hepatocyte growth factor-regulated substrate (Hrs) to sort the ubiquitinated cargo proteins from the early endosomes to the ESCRT-1 complex. ESCRT- 0 complex, STAM and Hrs, contains multiple ubiquitin binding domains, in which STAM has two ubiquitin binding domains, Vps27/Hrs/Stam (VHS) and ubiquitin interacting motif (UIM) at its N-terminus. By the cooperation of the multiple ubiquitin binding domains, the ESCRT-0 complex recognizes poly-ubiquitin, especially Lys63-linked ubiquitin. Here, we report the backbone resonance assignments and the secondary structure of the N-terminal 191 amino acids of the human STAM1 which includes the VHS domain and UIM. The {1H}-15N heteronuclear NOE experiments revealed that an unstructured and flexible loop region connects theVHS domain and UIM. Our work provides the basic information for the further NMR investigation of the interaction between STAM1 and poly-ubiquitin.
URI
http://pubs.kist.re.kr/handle/201004/38596
ISSN
1874-2718
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KIST Publication > Article
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