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Structural basis for Ufm1 recognition by UfSP
Structural highlights
FunctionUFSP_CAEEL Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ufm-1, a ubiquitin-like modifier protein bound to a number of target proteins (By similarity). Required, with oct-4, for the localization of a subset of 7 transmembrane domain odorant receptors, including odr-10, to the cilia of olfactory neurons AWA and AWC. Operates in aggregation behavior, and responses to oxygen levels.[UniProtKB:Q9NUQ7][1] [2] [3] Publication Abstract from PubMedUbiquitin and ubiquitin-like proteins (Ubls) are involved in a variety of cellular functions, and dysfunction of these proteins often leads to disease, thus requiring the precise molecular recognition of the partner. Here, we report a structural basis for the recognition of Ufm1 by the Ufm1-specific protease (UfSP), both from Caenorhabditis elegans. Ufm1 functions in endoplasmic reticulum homeostasis, cell cycle regulation, and dysfunctions of this protein can result in breast cancer and neurological disorders. The structure reveals that in addition to the extended beta-structure at the C-terminus of cUfm1, the interactions made by the completely conserved residues in Ufm1 orthologs, Pro88-Val92, corresponding to P6-P2 positions from the cleavage site, seem to be important for the specific recognition of Ufm1 by cUfSP. Structural basis for Ufm1 recognition by UfSP.,Kim KH, Ha BH, Kim EE FEBS Lett. 2018 Jan;592(2):263-273. doi: 10.1002/1873-3468.12951. Epub 2018 Jan, 4. PMID:29251776[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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