Proteomics

Dataset Information

0

Digly analysis of human Kv7.1 transfected in HEK293 cells. 


ABSTRACT: Polyubiquitin chain diversity generates a ‘ubiquitin code’ that universally regulates protein functional expression but functions of polyubiquitin diversity are mostly unknown. Using digly mass spectrometry, we have evaluated the basal polyubiquitin diversity on Kv7.1 ion channels expressed with a C-terminal YFP tag in HEK293 cells. Further, we co-expressed the E3 ligases NEDD4L and ITCH which downregulate Kv7.1 channels and investigated the change in polyubiquitin linkages on the channel.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Rajesh Soni  

LAB HEAD: Henry M. Colecraft

PROVIDER: PXD057805 | Pride | 2025-07-14

REPOSITORIES: Pride

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Publications

Decoding polyubiquitin regulation of K<sub>V</sub>7. 1 (KCNQ1) surface expression with engineered linkage-selective deubiquitinases.

Shanmugam Sri Karthika SK   Kanner Scott A SA   Zou Xinle X   Amarh Enoch E   Choudhury Papiya P   Soni Rajesh R   Kass Robert S RS   Colecraft Henry M HM  

Nature communications 20250701 1


Polyubiquitin chain diversity generates a 'ubiquitin code' that universally regulates protein abundance, localization, and function. Functions of polyubiquitin diversity are mostly unknown, with lack of progress due to an inability to selectively tune protein polyubiquitin linkages in live cells. We develop linkage-selective engineered deubiquitinases (enDUBs) by fusing linkage-selective DUB catalytic domains to GFP-targeted nanobody and use them to investigate polyubiquitin linkage regulation o  ...[more]

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