PSME3 regulates migration and differentiation of myoblasts
Kenneth D Kuhn, Ukrae H Cho, Martin W Hetzer
TL;DR
PSME3 helps control how muscle cells move and change during development, even without affecting overall gene activity.
Contribution
PSME3's role in regulating cell migration and differentiation through proteasome-independent mechanisms is newly identified.
Findings
PSME3 binds to active promoters during myogenesis but does not globally affect mRNA transcription.
PSME3 regulates adhesion-related proteins and cell motility via the HSP90 co-chaperone NUDC.
PSME3's function in myoblast differentiation is proteasome-independent.
Abstract
The noncanonical proteasome regulator PSME3 binds extensively to active promoters in undifferentiated myoblasts and regulates both cell migration and myotube formation during myogenesis. The acquisition of cellular identity requires large-scale alterations in cellular state. The noncanonical proteasome activator PSME3 is known to regulate diverse cellular processes, but its importance for differentiation remains unclear. Here, we demonstrate that PSME3 binds dynamically to highly active promoters over the course of differentiation. However, loss of PSME3 does not globally affect mRNA transcription. We find instead that PSME3 influences the levels of several adhesion-related proteins and acts upstream of the HSP90 co-chaperone NUDC to regulate cell motility and myoblast differentiation in a proteasome-independent manner. Our findings reveal several new facets of PSME3 functionality and…
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Taxonomy
TopicsUbiquitin and proteasome pathways · Nuclear Structure and Function · Heat shock proteins research