Proteomics

Dataset Information

0

AP-MS analysis of sirtuin-4 interactions in human fibroblasts


ABSTRACT: Sirtuins (SIRTs) form a critical family of nicotinamide adenine dinucleotide (NAD)-dependent enzymes that govern genome regulation, metabolism, and aging. Despite conserved deacetylase domains, SIRTs4-7 have little to no deacetylase activity, and a robust catalytic activity for mitochondrial SIRT4 has remained elusive. Moreover, in vitro characterization of SIRT4 has been hampered by difficulty in maintaining soluble and active recombinant protein. Therefore, to investigate potential cellular substrates of SIRT4, we used proteomics to define its mitochondrial protein interactions in human fibroblasts.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Fibroblast

SUBMITTER: Todd Greco  

LAB HEAD: Ileana Cristea

PROVIDER: PXD001447 | Pride | 2015-01-05

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
GFP_MITO_MOCK1_01.raw Raw
GFP_MITO_MOCK1_02.raw Raw
GFP_MITO_MOCK1_03.raw Raw
GFP_MITO_MOCK1_04.raw Raw
GFP_MITO_MOCK1_05.raw Raw
Items per page:
1 - 5 of 40
altmetric image

Publications


Sirtuins (SIRTs) are critical enzymes that govern genome regulation, metabolism, and aging. Despite conserved deacetylase domains, mitochondrial SIRT4 and SIRT5 have little to no deacetylase activity, and a robust catalytic activity for SIRT4 has been elusive. Here, we establish SIRT4 as a cellular lipoamidase that regulates the pyruvate dehydrogenase complex (PDH). Importantly, SIRT4 catalytic efficiency for lipoyl- and biotinyl-lysine modifications is superior to its deacetylation activity. PD  ...[more]

Similar Datasets

2016-03-04 | MSV000079557 | MassIVE
2024-06-20 | PXD044964 | Pride
2013-05-10 | E-GEOD-41415 | biostudies-arrayexpress
2021-09-08 | PXD017508 | Pride
2016-08-12 | PXD004212 | Pride
2020-06-12 | GSE152265 | GEO
2021-05-05 | MSV000087365 | GNPS
2019-02-25 | PXD012608 | Pride
2010-05-11 | GSE18488 | GEO
2023-10-24 | PXD033430 | Pride