Tiered Assembly of the Yeast Far3-7-8-9-10-11 Complex at the Endoplasmic Reticulum

Pracheil, Tammy; Liu, Zhengchang

doi:10.1074/jbc.m113.451674

Cited by 35 publications

(55 citation statements)

References 45 publications

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“…This fungal complex consists of the striatin homolog PRO11, the STRIP1/2 homolog PRO22, SmMOB3, and PP2A subunits. STRIPAK complexes from different systems contain further accessory components; among them is SLMAP, which interacts with distinct STRIPAK subunits and links STRIPAK subcomplexes to the nuclear envelope (22,51). We used BLAST (52) to search for an S. macrospora homolog of SLMAP (giԽ109731644) and identified SMAC_01224, which we termed PRO45 due to the phenotype of the mutant, as described below.…”

Section: Resultsmentioning

confidence: 99%

A Fungal Sarcolemmal Membrane-Associated Protein (SLMAP) Homolog Plays a Fundamental Role in Development and Localizes to the Nuclear Envelope, Endoplasmic Reticulum, and Mitochondria

et al. 2015

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bSarcolemmal 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. Membrane recruitment of protein complexes, cell signaling modules, and enzymes is a critical step for many cellular functions. The family of tail-anchored proteins is recognized for anchoring proteins and vesicles to specific membranes, such as the endoplasmic reticulum (ER) and the outer mitochondrial membrane (1), and tail-anchored proteins are characterized by a C-terminal single transmembrane domain, which is posttranslationally inserted into membranes (2, 3).Sarcolemmal membrane-associated protein (SLMAP) is a tailanchored protein first identified in myocardiac cells (4). In mammals, this protein is known to be involved in myoblast fusion during embryonic development, excitation-contraction coupling in cardiac myocytes, and cell cycle progression (5-8). Furthermore, SLMAP was identified to be a disease gene for Brugada syndrome, a cardiac channelopathy (9). The functional diversity of SLMAP is dependent on alternative splicing, leading to at least four different isoforms of the protein (4, 6, 7, 10). Importantly, gene expression analyses have implicated SLMAP misexpression with endothelial dysfunctions in diabetes, chromosomal aberrations, and cancer (11-14), and currently, SLMAP is the target of lectin-based treatment of drug-resistant cancer cells (15).SLMAP is conserved from yeasts to humans, and characterized fungal SLMAP homologs include Neurospora crassa HAM-4 (hyphal anastomosis 4), Saccharomyces cerevisiae Far9p (factor arrest 9p) and Far10p, as well as Schizosaccharomyces pombe Csc1p (component of SIP complex 1p) (16-18). HAM-4 is essential for vegetativ...

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Section: Resultsmentioning

confidence: 99%

A Fungal Sarcolemmal Membrane-Associated Protein (SLMAP) Homolog Plays a Fundamental Role in Development and Localizes to the Nuclear Envelope, Endoplasmic Reticulum, and Mitochondria

et al. 2015

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“…Although the FAR complex has been shown to be anchored on ER in yeast, whether this complex contributes to ER dynamics or function was not known (Pracheil and Liu, 2013). Our work reveals that C. elegans FARL-11, which is an ortholog of yeast FAR11, is present on ER and is essential for normal ER dynamics.…”

Section: Discussionmentioning

confidence: 77%

“…Our results reveal that PUF-8 promotes the germline expression of FARL-11, and that FARL-11 contributes to GSC proliferation by promoting GLP-1/Notch signaling. Further, we find that the C. elegans FARL-11, like its yeast counterpart FAR11, is localized on ER (Pracheil and Liu, 2013). Additionally, removal of FARL-11 alters ER morphology and considerably reduces the membrane localization of GLP-1, suggesting that FARL-11 is essential for ER form and function.…”

Section: Introductionmentioning

confidence: 75%

“…As shown in Fig. 6, FARL-11::GFP showed strong colocalization with mCherry::SP12 in the germline as well as in the embryo at different stages of the cell cycle, indicating that FARL-11 might indeed be localized on ER, like the yeast FAR complex (Pracheil and Liu, 2013).…”

Section: Farl-11 Is An Er Proteinmentioning

confidence: 92%

“…In yeast, FAR11 promotes PP2A phosphatase activity and antagonizes TOR signaling (Pracheil et al, 2012). FAR11 and PP2A are components of the FAR complex anchored on the ER (Pracheil and Liu, 2013). The Drosophila ortholog of FAR11 is also part of the fly STRIPAK PP2A complex, which negatively regulates Hippo signaling by reducing the levels of phosphorylated Hippo (Ribeiro et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

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A role for post-transcriptional control of ER dynamics and function in C. elegans germline stem cell maintenance

2016

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Membrane-bound receptors, which are crucial for mediating several key developmental signals, are synthesized on endoplasmic reticulum (ER). The functional integrity of ER must therefore be important for the regulation of at least some developmental programs. However, the developmental control of ER function is not well understood. Here, we identify the C. elegans protein FARL-11, an ortholog of the mammalian STRIPAK complex component STRIP1/2 (FAM40A/B), as an ER protein. In the C. elegans embryo, we find that FARL-11 is essential for the cell cycle-dependent morphological changes of ER and for embryonic viability. In the germline, FARL-11 is required for normal ER morphology and for membrane localization of the GLP-1/Notch receptor involved in germline stem cell (GSC) maintenance. Furthermore, we provide evidence that PUF-8, a key translational regulator in the germline, promotes the translation of farl-11 mRNA. These findings reveal that ER form and function in the C. elegans germline are post-transcriptionally regulated and essential for the niche-GSC signaling mediated by GLP-1.

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Fruiting-Body Development in Ascomycetes

Pöggeler¹,

Nowrousian²,

Teichert³

et al. 2018

Physiology and Genetics

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Tiered Assembly of the Yeast Far3-7-8-9-10-11 Complex at the Endoplasmic Reticulum

Cited by 35 publications

References 45 publications

A Fungal Sarcolemmal Membrane-Associated Protein (SLMAP) Homolog Plays a Fundamental Role in Development and Localizes to the Nuclear Envelope, Endoplasmic Reticulum, and Mitochondria

A Fungal Sarcolemmal Membrane-Associated Protein (SLMAP) Homolog Plays a Fundamental Role in Development and Localizes to the Nuclear Envelope, Endoplasmic Reticulum, and Mitochondria

A role for post-transcriptional control of ER dynamics and function in C. elegans germline stem cell maintenance

Fruiting-Body Development in Ascomycetes

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