A fungal sarcolemmal membrane-associated protein (SLMAP) homolog plays a fundamental role in development and localizes to the nuclear envelope, endoplasmic reticulum, and mitochondria

Sarcolemmal membrane-associated protein (SLMAP) is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. Further, SLMAP misexpression is associated with endothelial dysfunctions in diabetes and cancer. SLMAP...

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Bibliographic Details
Published in:Eukaryotic cell 2015-04, Vol.14 (4), p.345-358
Main Authors: Nordzieke, Steffen, Zobel, Thomas, Fränzel, Benjamin, Wolters, Dirk A, Kück, Ulrich, Teichert, Ines
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Endoplasmic Reticulum - physiology
Fungal Proteins - physiology
Hyphae - cytology
Membrane Proteins - physiology
Mitochondria - physiology
Models, Biological
Molecular Sequence Data
Nuclear Envelope - physiology
Protein Binding
Signal Transduction
Sordaria macrospora
Sordariales - cytology
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Summary:Sarcolemmal membrane-associated protein (SLMAP) is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. Further, SLMAP misexpression is associated with endothelial dysfunctions in diabetes and cancer. SLMAP is part of the conserved striatin-interacting phosphatase and kinase (STRIPAK) complex required for specific signaling pathways in yeasts, filamentous fungi, insects, and mammals. In filamentous fungi, STRIPAK was initially discovered in Sordaria macrospora, a model system for fungal differentiation. Here, we functionally characterize the STRIPAK subunit PRO45, a homolog of human SLMAP. We show that PRO45 is required for sexual propagation and cell-to-cell fusion and that its forkhead-associated (FHA) domain is essential for these processes. Protein-protein interaction studies revealed that PRO45 binds to STRIPAK subunits PRO11 and SmMOB3, which are also required for sexual propagation. Superresolution structured-illumination microscopy (SIM) further established that PRO45 localizes to the nuclear envelope, endoplasmic reticulum, and mitochondria. SIM also showed that localization to the nuclear envelope requires STRIPAK subunits PRO11 and PRO22, whereas for mitochondria it does not. Taken together, our study provides important insights into fundamental roles of the fungal SLMAP homolog PRO45 and suggests STRIPAK-related and STRIPAK-unrelated functions.
ISSN:1535-9778
1535-9786
DOI:10.1128/ec.00241-14