Proteomics

Dataset Information

0

Autophagy controls the protein composition of hair shafts


ABSTRACT: Hair shafts are formed by terminal differentiation of hair keratinocytes (trichocytes) in which keratins and keratin-associated proteins accumulate and undergo cross-linking. Here we tested the hypothesis that maturation of the hair shaft also involves the coordinated degradation of other proteins and, specifically, that this degradation is mediated by autophagy. To this end, we deleted the non-redundant autophagy regulator Atg7 in keratinocytes of the epidermis and skin appendages, including hair, and determined the proteome of hair shafts from fully autophagy-competent and epithelial autophagy-deficient mice. The abrogation of autophagy led to significantly increased abundance of proteins regulating house-keeping functions of the cell and a decrease of cytoskeletal proteins. Translation factors, tRNA-ligases, ribosomal proteins and the components of proteasomes were particularly elevated in the absence of autophagy, indicating a central role of autophagy in regulating multiple steps of protein turnover in hair keratinocytes. These results demonstrate that hair keratinocytes depend on autophagy for establishing the mature protein composition of hair.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Mus Musculus (ncbitaxon:10090)

SUBMITTER: Robert H. Rice  

PROVIDER: MSV000091072 | MassIVE | Tue Jan 17 10:49:00 GMT 2023

SECONDARY ACCESSION(S): PXD039530

REPOSITORIES: MassIVE

Similar Datasets

2017-02-14 | GSE84935 | GEO
2021-12-31 | GSE149653 | GEO
2022-11-03 | PXD037830 | JPOST Repository
2010-09-03 | GSE19309 | GEO
2010-09-03 | E-GEOD-19309 | biostudies-arrayexpress
2024-01-10 | GSE229890 | GEO
2022-07-02 | GSE193269 | GEO
2023-01-25 | GSE223219 | GEO
2016-02-29 | E-MTAB-4535 | biostudies-arrayexpress
2017-05-15 | E-GEOD-29547 | biostudies-arrayexpress