Genes encoding a striatin-like protein (ham-3) and a forkhead associated protein (ham-4) are required for hyphal fusion in Neurospora crassa

Simonin, Anna; Rasmussen, Carolyn G.; Yang, Mabel; Glass, N. Louise

doi:10.1016/j.fgb.2010.06.010

Cited by 68 publications

(95 citation statements)

References 65 publications

(82 reference statements)

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“…In Saccharomyces cerevisiae, Far8 (striatin), Far11 (STRIP1/2), Vps64/Far10 (orthologous to the alternate STRI-PAK component SLMAP), along with Far3 and Far7 (for which no human orthologs are known) form a protein complex implicated in cell cycle arrest following pheromone treatment (38). Orthologs of these ancestral STRIPAK genes are required for proper vegetative membrane fusion in filamentous fungi (39,40). The function of STRIPAK in mediating membrane fusion appears to have been conserved in mammals, as deregulation of SLMAP prevents myoblast fusion to myotubes (41).…”

Section: Discussionmentioning

confidence: 99%

Structure-Function Analysis of Core STRIPAK Proteins

Kean

Ceccarelli

Goudreault

et al. 2011

Journal of Biological Chemistry

132

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We show that striatins and CCM3 regulate the Golgi localization of MST4 in an opposite manner. Consistent with a previously described function for MST4 and CCM3 in Golgi positioning, depletion of CCM3 or striatins affects Golgi polarization, also in an opposite manner. We propose that STRIPAK regulates the balance between MST4 localization at the Golgi and in the cytosol to control Golgi positioning.

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Section: Discussionmentioning

confidence: 99%

Structure-Function Analysis of Core STRIPAK Proteins

Kean

Ceccarelli

Goudreault

et al. 2011

Journal of Biological Chemistry

132

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“…Genes important for germling/hyphal fusion include genes of the MAK-2 MAP kinase pathway and upstream factors (Fu et al 2011;Dettmann et al 2014), members of the cell wall integrity (CWI) MAP kinase pathway (Fu et al 2011(Fu et al , 2014, the STRIPAK complex (Simonin et al 2010;Dettmann et al 2013), the NADPH oxidation complex (Cano-Dominguez et al 2008;Fu et al 2011Fu et al , 2014, a number of transcription factors (Aldabbous et al 2010;Fu et al 2011;Leeder et al 2013), and genes encoding uncharacterized proteins (Fu et al 2011(Fu et al , 2014. Previously, we showed that HAM-5-GFP localizes to puncta in Dmak-2, Dham-7, and Dham-11 fusion mutants (Jonkers et al 2014).…”

Section: Ham-5 Localization Is Not Disrupted In Other Fusion Mutantsmentioning

confidence: 99%

Chemotropism and Cell Fusion in Neurospora crassa Relies on the Formation of Distinct Protein Complexes by HAM-5 and a Novel Protein HAM-14

et al. 2016

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In filamentous fungi, communication is essential for the formation of an interconnected, multinucleate, syncytial network, which is constructed via hyphal fusion or fusion of germinated asexual spores (germlings). Anastomosis in filamentous fungi is comparable to other somatic cell fusion events resulting in syncytia, including myoblast fusion during muscle differentiation, macrophage fusion, and fusion of trophoblasts during placental development. In Neurospora crassa, fusion of genetically identical germlings is a highly dynamic and regulated process that requires components of a MAP kinase signal transduction pathway. The kinase pathway components (NRC-1, MEK-2 and MAK-2) and the scaffold protein HAM-5 are recruited to hyphae and germling tips undergoing chemotropic interactions. The MAK-2/HAM-5 protein complex shows dynamic oscillation to hyphae/germling tips during chemotropic interactions, and which is out-of-phase to the dynamic localization of SOFT, which is a scaffold protein for components of the cell wall integrity MAP kinase pathway. In this study, we functionally characterize HAM-5 by generating ham-5 truncation constructs and show that the N-terminal half of HAM-5 was essential for function. This region is required for MAK-2 and MEK-2 interaction and for correct cellular localization of HAM-5 to "fusion puncta." The localization of HAM-5 to puncta was not perturbed in 21 different fusion mutants, nor did these puncta colocalize with components of the secretory pathway. We also identified HAM-14 as a novel member of the HAM-5/MAK-2 pathway by mining MAK-2 phosphoproteomics data. HAM-14 was essential for germling fusion, but not for hyphal fusion. Colocalization and coimmunoprecipitation data indicate that HAM-14 interacts with MAK-2 and MEK-2 and may be involved in recruiting MAK-2 (and MEK-2) to complexes containing HAM-5.KEYWORDS cell fusion; Neurospora crassa; MAP kinase signaling; protein complexes; chemotropism F USION between genetically identical cells exists in many organisms and plays an important role in different developmental processes, for example, myoblast fusion during the formation of muscle tissue, macrophage fusion, or fusion of trophoblasts in placental development (Chen and Olson 2005;Aguilar et al. 2013). In fungi, vegetative fusion enables a fungal colony to share resources and has implications for fitness and virulence (Craven et al. 2008;Fricker et al. 2009;Eaton et al. 2011;Richard et al. 2012;Simonin et al. 2012;Roper et al. 2013;Chagnon 2014). In the filamentous ascomycete fungus, Neurospora crassa, genetically identical germinated asexual spores (germlings) undergo fusion to form a syncytium that is an interconnected network of fused cells Leeder et al. 2013;Herzog et al. 2015). An important pathway required for both germling and hyphal fusion is a conserved mitogen-activated protein kinase (MAPK) cascade that includes the MAPK kinase kinase NRC-1, the MAPK kinase MEK-2, the MAPK MAK-2, and the scaffold protein, HAM-5 (Pandey et al. 2004;Dettmann et al. 2012Dettm...

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“…The CATs select their partners at a distance as evidenced by their purposeful homing toward each other that becomes apparent when their separation is less than $15 mm. Genetic analyses identified a number of candidate genes whose products were required for CAT formation, homing and fusion [14][15][16][17][18][19]. Deletion of the gene encoding the MAP kinase MAK-2 resulted in cells unable to chemotropically home and fuse with other, even normal, wild-type, cells.…”

Section: Introductionmentioning

confidence: 99%

Excitable behavior can explain the “ping‐pong” mode of communication between cells using the same chemoattractant

et al. 2012

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Here we elucidate a paradox: how a single chemoattractant-receptor system in two individuals is used for communication despite the seeming inevitability of self-excitation. In the filamentous fungus Neurospora crassa, genetically identical cells that produce the same chemoattractant fuse via the homing of individual cell protrusions toward each other. This is achieved via a recently described ''ping-pong'' pulsatile communication. Using a generic activatorinhibitor model of excitable behavior, we demonstrate that the pulse exchange can be fully understood in terms of two excitable systems locked into a stable oscillatory pattern of mutual excitation. The most puzzling properties of this communication are the sudden onset of oscillations with final amplitude, and the absence of seemingly inevitable self-excitation. We show that these properties result directly from both the excitability threshold and refractory period characteristic of excitable systems. Our model suggests possible molecular mechanisms for the ping-pong communication.

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Genes encoding a striatin-like protein (ham-3) and a forkhead associated protein (ham-4) are required for hyphal fusion in Neurospora crassa

Cited by 68 publications

References 65 publications

Structure-Function Analysis of Core STRIPAK Proteins

Structure-Function Analysis of Core STRIPAK Proteins

Chemotropism and Cell Fusion in Neurospora crassa Relies on the Formation of Distinct Protein Complexes by HAM-5 and a Novel Protein HAM-14

Excitable behavior can explain the “ping‐pong” mode of communication between cells using the same chemoattractant

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