FARL-11 (STRIP1/2) is required for sarcomere and sarcoplasmic reticulum organization in C. elegans

Protein phosphatase 2A (PP2A) functions in a variety of cellular contexts. PP2A can assemble into four different complexes based on the inclusion of different regulatory or targeting subunits. The B''' regulatory subunit "striatin" forms the STRIPAK complex consisting of str...

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Bibliographic Details
Published in:Molecular biology of the cell 2023-08, Vol.34 (9), p.ar86-ar86
Main Authors: Martin, Sterling C T, Qadota, Hiroshi, Oberhauser, Andres F, Hardin, Jeff, Benian, Guy M
Format: Article
Language:English
Subjects:
Animals
Caenorhabditis elegans
Caenorhabditis elegans - metabolism
Endoplasmic Reticulum - metabolism
Genetic aspects
Identification and classification
Phenotype
Physiological aspects
Protein Phosphatase 2 - metabolism
Sarcomeres - metabolism
Sarcoplasmic Reticulum - metabolism
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Summary:Protein phosphatase 2A (PP2A) functions in a variety of cellular contexts. PP2A can assemble into four different complexes based on the inclusion of different regulatory or targeting subunits. The B''' regulatory subunit "striatin" forms the STRIPAK complex consisting of striatin, a catalytic subunit (PP2AC), striatin-interacting protein 1 (STRIP1), and MOB family member 4 (MOB4). In yeast and , STRIP1 is required for formation of the endoplasmic reticulum (ER). Because the sarcoplasmic reticulum (SR) is the highly organized muscle-specific version of ER, we sought to determine the function of the STRIPAK complex in muscle using . CASH-1 (striatin) and FARL-11 (STRIP1/2) form a complex in vivo, and each protein is localized to SR. Missense mutations and single amino acid losses in and each result in similar sarcomere disorganization. A missense mutation in shows no detectable FARL-11 protein by immunoblot, disruption of SR organization around M-lines, and altered levels of the SR Ca release channel UNC-68.
ISSN:1059-1524
1939-4586
DOI:10.1091/mbc.E23-03-0083