Dataset Information

Insights into the regulation of CHIP E3 ligase-mediated ubiquitination of neuronal protein BNIP-H

ABSTRACT: The project aims to characterize the protein-protein interactions of CHIP and BNIP-H proteins, which are associated with autoubiquitination. To determine the mechanism of action both proteins were expressed as wild-types and mutants.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Nikhil Kumar Tulsian

LAB HEAD: Jayaraman Sivaraman

PROVIDER: PXD054896 | Pride | 2025-05-07

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	08Jun21_NKT_BNIP-wt_UnD1_IA_final_peptide.csv	Csv
	08Jun21_NKT_BNIP-wt_UnD2_IA_final_peptide.csv	Csv
	08Jun21_NKT_BNIP-wt_UnD3_IA_final_peptide.csv	Csv
	11Jun21_NKT_CHIP-9M_UnD1_IA_final_peptide.csv	Csv
	11Jun21_NKT_CHIP-9M_UnD3_IA_final_peptide.csv	Csv

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Publications

Insights into the regulation of CHIP E3 ligase-mediated ubiquitination of neuronal protein BNIP-H.

Shankar Srihari S Liu Yaochen Y Tulsian Nikhil Kumar NK Low Boon C BC Lin Qingsong Q Sivaraman J J

PNAS nexus 20241125 12

BCL2/adenovirus E1B 19-kDa protein-interacting protein 2 homolog (BNIP-H or Caytaxin), a pivotal adaptor protein that facilitates cerebellar cortex growth and synaptic transmission, is posttranslationally modified to regulate neuronal function. This study reports the ubiquitination of BNIP-H by Carboxyl terminus of Hsc70-Interacting Protein (CHIP), a U-box containing E3 ligase that is also regulated <i>via</i> autoubiquitination. Specifically, it was observed that CHIP autoubiquitinated itself p ...[more]

PMID: 39703232

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