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Lactylation stabilizes TFEB to elevate autophagy and lysosomal activity

ABSTRACT: To identify the interaction proteins of TFEB, HEK293T cells transiently expressing TFEB-Flag were immunoprecipitated with anti-Flag beads. The beeds were used to do a LC/MS.

ORGANISM(S): Homo Sapiens

SUBMITTER: Wei Liu

PROVIDER: PXD050578 | iProX | Wed Mar 13 00:00:00 GMT 2024

REPOSITORIES: iProX

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Lactylation stabilizes TFEB to elevate autophagy and lysosomal activity.

Huang Yewei Y Luo Gan G Peng Kesong K Song Yue Y Wang Yusha Y Zhang Hongtao H Li Jin J Qiu Xiangmin X Pu Maomao M Liu Xinchang X Peng Chao C Neculai Dante D Sun Qiming Q Zhou Tianhua T Huang Pintong P Liu Wei W

The Journal of cell biology 20240828 11

The transcription factor TFEB is a major regulator of lysosomal biogenesis and autophagy. There is growing evidence that posttranslational modifications play a crucial role in regulating TFEB activity. Here, we show that lactate molecules can covalently modify TFEB, leading to its lactylation and stabilization. Mechanically, lactylation at K91 prevents TFEB from interacting with E3 ubiquitin ligase WWP2, thereby inhibiting TFEB ubiquitination and proteasome degradation, resulting in increased TF ...[more]

PMID: 39196068

Similar Datasets

Lactylation stabilizes TFEB to elevate autophagy and lysosomal activity.

Project description:The transcription factor TFEB is a major regulator of lysosomal biogenesis and autophagy. There is growing evidence that posttranslational modifications play a crucial role in regulating TFEB activity. Here, we show that lactate molecules can covalently modify TFEB, leading to its lactylation and stabilization. Mechanically, lactylation at K91 prevents TFEB from interacting with E3 ubiquitin ligase WWP2, thereby inhibiting TFEB ubiquitination and proteasome degradation, resulting in increased TFEB activity and autophagy flux. Using a specific antibody against lactylated K91, enhanced TFEB lactylation was observed in clinical human pancreatic cancer samples. Our results suggest that lactylation is a novel mode of TFEB regulation and that lactylation of TFEB may be associated with high levels of autophagy in rapidly proliferating cells, such as cancer cells.

| S-EPMC11354204 | biostudies-literature

Identify the proteins interacting with STX17

Project description:To identify the specific proteins interacting with STX17, HEK293T cells stably expressing Flag-STX17 were lysed and immunoprecipitated with anti-Flag antibody, and eluted for Commassie blue staining and then subjected to mass spectrometric analysis.

2023-06-24 | PXD041897 | Pride

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Project description:ChIP-seq analysis of the HEK293T cell line transiently expressing various FLAG-tagged proteins

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Mass spectrometry runs and analysis of host proteins co-immunoprecipitated with RABV M protein

Project description:To explore the role of the matrix protein in RABV infection of host cells, we looked for host proteins that interact with the RABV M protein. We performed Flag-tag-based immunoprecipitation of lysates of HEK293T cells transfected with plasmids expressing either N- or C-terminally Flag-tagged M protein (M-NF or M-CF, respectively), and identified host proteins that interacted with the M proteins by using mass spectrometry (MS). Proteins were detected in lysates of cells transfected with the plasmid expressing Flag-tagged M proteins but not in those of cells transfected with the control plasmid. We identified a total of 2,672 host proteins that co-immunoprecipitated with the M protein; 492 proteins co-immunoprecipitated to both M-NF and M-CF, 1,761 proteins co-immunoprecipitated with M-NF only, and 419 proteins co-immunoprecipitated with M-CF only.

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Identify METTL3, 14 and 16-bound transcripts via RIP-seq

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2021-10-28 | GSE156797 | GEO

CLIP-seq analysis of hnRNPA1-RNA interactions

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CYP1B1-AS1 regulates CYP1B1 to promote Coxiella burnetii pathogenesis by inhibiting ROS and host cell death

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2024-12-23 | MSV000096725 | MassIVE

"LRRK2: Autophagy and Lysosomal Activity".

Project description:It has been 15 years since the Leucine-rich repeat kinase 2 (LRRK2) gene was identified as the most common genetic cause for Parkinson's disease (PD). The two most common mutations are the LRRK2-G2019S, located in the kinase domain, and the LRRK2-R1441C, located in the ROC-COR domain. While the LRRK2-G2019S mutation is associated with increased kinase activity, the LRRK2-R1441C exhibits a decreased GTPase activity and altered kinase activity. Multiple lines of evidence have linked the LRRK2 protein with a role in the autophagy pathway and with lysosomal activity in neurons. Neurons rely heavily on autophagy to recycle proteins and process cellular waste due to their post-mitotic state. Additionally, lysosomal activity decreases with age which can potentiate the accumulation of ?-synuclein, the pathological hallmark of PD, and subsequently lead to the build-up of Lewy bodies (LBs) observed in this disorder. This review provides an up to date summary of the LRRK2 field to understand its physiological role in the autophagy pathway in neurons and related cells. Careful assessment of how LRRK2 participates in the regulation of phagophore and autophagosome formation, autophagosome and lysosome fusion, lysosomal maturation, maintenance of lysosomal pH and calcium levels, and lysosomal protein degradation are addressed. The autophagy pathway is a complex cellular process and due to the variety of LRRK2 models studied in the field, associated phenotypes have been reported to be seemingly conflicting. This review provides an in-depth discussion of different models to assess the normal and disease-associated role of the LRRK2 protein on autophagic function. Given the importance of the autophagy pathway in Parkinson's pathogenesis it is particularly relevant to focus on the role of LRRK2 to discover novel therapeutic approaches that restore lysosomal protein degradation homeostasis.

| S-EPMC7262160 | biostudies-literature

Identification of proteins that interacted with ESCO2

Project description:The Flag–ESCO2 plasmids were transfected into HEK293T cells, Flag–ESCO2 complexes were co-immunoprecipitated using an anti-Flag antibody. The Flag–ESCO2 complexes was separated using SDS PAGE, and then was identified by combining silver staining and mass spectrometry.

2021-09-10 | PXD023527 | Pride

Site mapping of PGK1 O-GlcNAcylation

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2019-11-06 | PXD015659 | Pride

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