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A novel function of the monomeric CCT epsilon subunit connects the serum response factor pathway to chaperone-mediated actin folding

Artikel i vetenskaplig tidskrift
Författare Kerryn Elliott
Andreas Svanstrom
M. Spiess
R. Karlsson
Julie Grantham
Publicerad i Molecular Biology of the Cell
Volym 26
Nummer/häfte 15
Sidor 2801-2809
ISSN 1059-1524
Publiceringsår 2015
Publicerad vid Institutionen för kemi och molekylärbiologi
Sidor 2801-2809
Språk en
Länkar dx.doi.org/10.1091/mbc.E15-01-0048
Ämnesord CYTOSOLIC CHAPERONIN, SUBSTRATE-BINDING, TUBULIN, COMPLEX, COACTIVATOR, GELSOLIN, DOMAIN, CELLS
Ämneskategorier Klinisk medicin

Sammanfattning

Correct protein folding is fundamental for maintaining protein homeostasis and avoiding the formation of potentially cytotoxic protein aggregates. Although some proteins appear to fold unaided, actin requires assistance from the oligomeric molecular chaperone CCT. Here we report an additional connection between CCT and actin by identifying one of the CCT subunits, CCT epsilon, as a component of the myocardin-related cotranscription factor-A (MRTF-A)/serum response factor (SRF) pathway. The SRF pathway registers changes in G-actin levels, leading to the transcriptional up-regulation of a large number of genes after actin polymerization. These genes encode numerous actin-binding proteins as well as actin. We show that depletion of the CCT epsilon subunit by siRNA enhances SRF signaling in cultured mammalian cells by an actin assembly-independent mechanism. Overexpression of CCTe in its monomeric form revealed that CCT epsilon binds via its substrate-binding domain to the C-terminal region of MRTF-A and that CCT epsilon is able to alter the nuclear accumulation of MRTF-A after stimulation by serum addition. Given that the levels of monomeric CCT epsilon conversely reflect the levels of CCT oligomer, our results suggest that CCT epsilon provides a connection between the actin-folding capacity of the cell and actin expression.

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