Drosophila p38 MAPK interacts with BAG‐3/starvin to regulate age‐dependent protein homeostasis

As organisms age, they often accumulate protein aggregates that are thought to be toxic, potentially leading to age‐related diseases. This accumulation of protein aggregates is partially attributed to a failure to maintain protein homeostasis. A variety of genetic factors have been linked to longevi...

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Published in:	Aging cell Vol. 20; no. 11; pp. e13481 - n/a
Main Authors:	Ryan, Sarah M., Almassey, Michael, Burch, Amelia M., Ngo, Gia, Martin, Julia M., Myers, David, Compton, Devin, Archie, Shira, Cross, Megan, Naeger, Lauren, Salzman, Ashley, Virola‐Iarussi, Alyssa, Barbee, Scott A., Mortimer, Nathan T., Sanyal, Subhabrata, Vrailas‐Mortimer, Alysia D.
Format:	Journal Article
Language:	English
Published:	England John Wiley & Sons, Inc 01-11-2021 John Wiley and Sons Inc
Subjects:	Age Aging Aging - genetics Aging - metabolism Animals Animals, Genetically Modified Autophagy BAG‐3/starvin Drosophila melanogaster - genetics Drosophila melanogaster - metabolism Drosophila Proteins - genetics Drosophila Proteins - metabolism Female Gene Deletion Genetic factors Homeostasis Insects Kinases Lamin Lamins - metabolism Life span Locomotion - genetics Longevity - genetics Macroautophagy - genetics Mammals MAP kinase MAP Kinase Signaling System - genetics Muscles - metabolism Original Paper Original Papers Oxidative stress Oxidative Stress - genetics p38 MAPK p38 Mitogen-Activated Protein Kinases - genetics p38 Mitogen-Activated Protein Kinases - metabolism Phenotype protein aggregation Protein interaction Proteins Proteolysis Proteostasis - genetics Quality control RNA Interference Lamin aging BAG-3/starvin p38 MAPK protein aggregation
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Summary:	As organisms age, they often accumulate protein aggregates that are thought to be toxic, potentially leading to age‐related diseases. This accumulation of protein aggregates is partially attributed to a failure to maintain protein homeostasis. A variety of genetic factors have been linked to longevity, but how these factors also contribute to protein homeostasis is not completely understood. In order to understand the relationship between aging and protein aggregation, we tested how a gene that regulates lifespan and age‐dependent locomotor behaviors, p38 MAPK (p38Kb), influences protein homeostasis as an organism ages. We find that p38Kb regulates age‐dependent protein aggregation through an interaction with starvin, a regulator of muscle protein homeostasis. Furthermore, we have identified Lamin as an age‐dependent target of p38Kb and starvin. We find that p38 MAPK (p38Kb) regulates age‐dependent protein homeostasis through an interaction with the BAG protein, starvin. In addition, we find that Lamin Dm0, a homologue of the aging gene Lamin A/C, is a target of p38Kb and stv for degradation during aging.
Bibliography:	Sarah M. Ryan and Michael Almassey contributed equally to this work. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1474-9718 1474-9726
DOI:	10.1111/acel.13481