scholarly journals Roles of fission yeast tea1p in the localization of polarity factors and in organizing the microtubular cytoskeleton

2002 ◽  
Vol 157 (5) ◽  
pp. 783-793 ◽  
Author(s):  
Ralf Behrens ◽  
Paul Nurse
Keyword(s):  
Cell Growth ◽  
Yeast Cell ◽  
Fission Yeast ◽  
Coiled Coil ◽  
Live Imaging ◽  
Cylindrical Shape ◽  
Polarized Growth ◽  
Coiled Coil Domain ◽  
Straight Line ◽  
Microtubular Cytoskeleton

The cylindrical shape of the fission yeast cell is generated by linear polarized growth from its cell ends. Using immunofluorescence and live imaging microscopy, we have investigated the roles of the cell end marker tea1p in generating linear polarized growth. We found that tea1p is primarily transported on plus ends of microtubules from the vicinity of the nucleus to the cell ends, and that its movement near the nucleus is independent of the kinesin tea2p. Deletion analysis identified a coiled-coil domain in tea1p essential for its retention at cell ends, and demonstrated that tea1p exerts different functions dependent on its location. On the tips of microtubules, tea1p prevents the curling of microtubules around the cell ends, whereas it is required for maintaining linear cell growth and for retention of polarity factors such as the Dyrk kinase pom1p, the CLIP170-like tip1p, and tea2p at the cell ends. We propose that tea1p has roles in organizing the microtubule cytoskeleton on the tips of microtubules, and in the retention of factors at the cell ends necessary for the cell to grow in a straight line.

scholarly journals The git5 Gβ and git11 Gγ Form an Atypical Gβγ Dimer Acting in the Fission Yeast Glucose/cAMP Pathway

Genetics ◽  
2001 ◽  
Vol 157 (3) ◽  
pp. 1159-1168 ◽  
Author(s):  
Sheila Landry ◽  
Charles S Hoffman
Keyword(s):  
Fission Yeast ◽  
Mammalian Cells ◽  
Glucose Repression ◽  
Coiled Coil ◽  
Carboxy Terminus ◽  
Amino Terminal ◽  
Camp Pathway ◽  
Coiled Coil Domain ◽  
Mutational Activation ◽  
Two Hybrid

AbstractFission yeast adenylate cyclase, like mammalian adenylate cyclases, is regulated by a heterotrimeric G protein. The gpa2 Gα and git5 Gβ are both required for glucose-triggered cAMP signaling. The git5 Gβ is a unique member of the Gβ family in that it lacks an amino-terminal coiled-coil domain shown to be essential for mammalian Gβ folding and interaction with Gγ subunits. Using a git5 bait in a two-hybrid screen, we identified the git11 Gγ gene. Co-immunoprecipitation studies confirm the composition of this Gβγ dimer. Cells deleted for git11 are defective in glucose repression of both fbp1 transcription and sexual development, resembling cells lacking either the gpa2 Gα or the git5 Gβ. Overexpression of the gpa2 Gα partially suppresses loss of either the git5 Gβ or the git11 Gγ, while mutational activation of the Gα fully suppresses loss of either Gβ or Gγ. Deletion of gpa2 (Gα), git5 (Gβ), or git11 (Gγ) confer quantitatively distinct effects on fbp1 repression, indicating that the gpa2 Gα subunit remains partially active in the absence of the Gβγ dimer and that the git5 Gβ subunit remains partially active in the absence of the git11 Gγ subunit. The addition of the CAAX box from the git11 Gγ to the carboxy-terminus of the git5 Gβ partially suppresses the loss of the Gγ. Thus the Gγ in this system is presumably required for localization of the Gβγ dimer but not for folding of the Gβ subunit. In mammalian cells, the essential roles of the Gβ amino-terminal coiled-coil domains and Gγ partners in Gβ folding may therefore reflect a mechanism used by cells that express multiple forms of both Gβ and Gγ subunits to regulate the composition and activity of its G proteins.

scholarly journals Cortical tethering of mitochondria by the dynein anchor Mcp5 enables uniparental mitochondrial inheritance during fission yeast meiosis

2019 ◽  
Author(s):  
Kritika Mehta ◽  
Vaishnavi Ananthanarayanan
Keyword(s):  
Mitochondrial Dna ◽  
Fission Yeast ◽  
Coiled Coil ◽  
The Other ◽  
Uniparental Inheritance ◽  
Zygote Formation ◽  
Mitochondrial Inheritance ◽  
Distinct Mechanism ◽  
Coiled Coil Domain ◽  
Yeast Meiosis

SummaryDuring sexual reproduction in eukaryotes, processes such as active degradation and dilution of paternal mitochondria ensure maternal mitochondrial inheritance. In the isogamous organism fission yeast, we employed high-resolution fluorescence microscopy to visualize mitochondrial inheritance during meiosis by differentially labeling mitochondria of the two parental cells. Remarkably, mitochondria, and thereby, mitochondrial DNA from the parental cells did not mix upon zygote formation, but remained segregated at the poles by attaching to clusters of the dynein anchor Mcp5 via its coiled-coil domain. We observed that this tethering of parental mitochondria to the poles results in uniparental inheritance of mitochondria, wherein two of the four spores formed subsequently contained mitochondria from one parent and the other spores, mitochondria from the other parent. Further, the presence of dynein on an Mcp5 cluster precluded the attachment of mitochondria to the same cluster. Taken together, we reveal a distinct mechanism that achieves uniparental inheritance by segregation of parental mitochondria.

scholarly journals Coiled-Coil Domain Containing 80 Suppresses Nonylphenol-Induced Colorectal Cancer Cell Proliferation by Inhibiting the Activation of ERK1/2

2021 ◽  
Vol 9 ◽  
Author(s):  
Jing Wang ◽  
Yuan-wei Zhang ◽  
Nian-jie Zhang ◽  
Shuo Yin ◽  
Du-ji Ruan ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Cell Proliferation ◽  
Cell Growth ◽  
Differentially Expressed Genes ◽  
Endocrine Disrupting Chemicals ◽  
Coiled Coil ◽  
Underlying Mechanism ◽  
Differentially Expressed ◽  
Coiled Coil Domain ◽  
Upregulated Genes

Recently, the effect of endocrine-disrupting chemicals on the cancer procession has been a concern. Nonylphenol (NP) is a common environmental estrogen that has been shown to enhance the proliferation of colorectal cancer (CRC) cells in our previous studies; however, the underlying mechanism remains unclear. In this study, we confirmed the increased concentration of NP in the serum of patients with CRC. RNA sequencing was used to explore the differentially expressed genes after NP exposure. We found 16 upregulated genes and 12 downregulated genes in COLO205 cells after NP treatment. Among these differentially expressed genes, we found that coiled-coil domain containing 80 (CCDC80) was downregulated by NP treatment and was associated with CRC progression. Further experiments revealed that the overexpression of CCDC80 significantly suppressed NP-induced cell proliferation and recovered the reduced cell apoptosis. Meanwhile, the overexpression of CCDC80 significantly inhibited the activation of ERK1/2 induced by NP treatment. ERK1/2 inhibitor (PD98059) treatment also suppressed NP-induced CRC cell growth, but the overexpression of CCDC80 did not enhance the effect of ERK1/2 inhibitor. Taken together, NP treatment significantly inhibited the expression of CCDC80, and the overexpression of CCDC80 suppressed NP-induced CRC cell growth by inhibiting the activation of ERK1/2. These results suggest that NP could induce CRC cell growth by influencing the expression of multiple genes. CCDC80 and ERK1/2 inhibitors may be suitable therapeutic targets in NP-related CRC progression.

Cdc42 regulates polarized growth and cell integrity in fission yeast

2014 ◽  
Vol 42 (1) ◽  
pp. 201-205 ◽  
Author(s):  
Sergio A. Rincón ◽  
Miguel Estravís ◽  
Pilar Pérez
Keyword(s):  
Cell Growth ◽  
Fission Yeast ◽  
Rho Gtpase ◽  
Short Review ◽  
Model Systems ◽  
Polarized Growth ◽  
Cell Integrity ◽  
Polarized Cell Growth ◽  
New Material ◽  
High Level

Polarized cell growth requires a well-orchestrated number of events, namely selection of growth site, organization of cytoskeleton elements and delivery of new material to the growth region. The small Rho GTPase Cdc42 has emerged as a major organizer of polarized growth through its participation in many of these events. In the present short review, we focus on the regulation of Cdc42 activity and localization as well as how it controls downstream events necessary for polarized cell growth in Schizosaccharomyces pombe. Owing to the high level of similarity of the polarity pathways, analogies between fission yeast and other model systems can be useful to decipher how cells can actively define their shape by polarized growth.

scholarly journals Pea2 protein of yeast is localized to sites of polarized growth and is required for efficient mating and bipolar budding.

1996 ◽  
Vol 135 (3) ◽  
pp. 725-739 ◽  
Author(s):  
N Valtz ◽  
I Herskowitz
Keyword(s):  
Coiled Coil ◽  
Cell Types ◽  
Cell Polarization ◽  
Polarized Growth ◽  
Coiled Coil Domain ◽  
Cell Biol ◽  
Two Phases ◽  
Diploid Cells ◽  
Novel Protein

Saccharomyces cerevisiae exhibits polarized growth during two phases of its life cycle, budding and mating. The site for polarization during vegetative growth is determined genetically: a and alpha haploid cells exhibit an axial budding pattern, and a/alpha diploid cells exhibit a bipolar pattern. During mating, each cell polarizes towards its partner to ensure efficient mating. SPA2 is required for the bipolar budding pattern (Snyder. M 1989. J. Cell Biol. 108:1419-1429; Zahner, J.A., H.A. Harkins, and J.R. Pringle. 1996. Mol. Cell. Biol. 16:1857-1870) and polarization during mating (Snyder, M., S. Gehrung, and B.D. Page. 1991. J. Cell Biol. 114: 515-532). We previously identified mutants defective in PEA2 and SPA2 which alter cell polarization in the presence of mating pheromone in a similar manner (Chenevert, J., N. Valtz, and I. Herskowitz. 1994. Genetics, 136:1287-1297). Here we report the further characterization of these mutants. We have found that PEA2 is also required for the bipolar budding pattern and that it encodes a novel protein with a predicted coiled-coil domain. Pea2p is expressed in all cell types and is localized to sites of polarized growth in budding and mating cells in a pattern similar to Spa2p, Pea2p and Spa2p exhibit interdependent localization: Spa2p is produced in pea2 mutants but fails to localize properly; Pea2p is not stably produced in spa2 mutants. These results suggest that Pea2p and Spa2p function together as a complex to generate the bipolar budding pattern and to guarantee proper polarization during mating.

TMCC3 localizes at the three-way junctions for the proper tubular network of the endoplasmic reticulum

2019 ◽  
Vol 476 (21) ◽  
pp. 3241-3260
Author(s):  
Sindhu Wisesa ◽  
Yasunori Yamamoto ◽  
Toshiaki Sakisaka
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Mammalian Cells ◽  
Coiled Coil ◽  
Transmembrane Domains ◽  
Domain Family ◽  
Coiled Coil Domain ◽  
U2os Cells ◽  
Er Membrane

The tubular network of the endoplasmic reticulum (ER) is formed by connecting ER tubules through three-way junctions. Two classes of the conserved ER membrane proteins, atlastins and lunapark, have been shown to reside at the three-way junctions so far and be involved in the generation and stabilization of the three-way junctions. In this study, we report TMCC3 (transmembrane and coiled-coil domain family 3), a member of the TEX28 family, as another ER membrane protein that resides at the three-way junctions in mammalian cells. When the TEX28 family members were transfected into U2OS cells, TMCC3 specifically localized at the three-way junctions in the peripheral ER. TMCC3 bound to atlastins through the C-terminal transmembrane domains. A TMCC3 mutant lacking the N-terminal coiled-coil domain abolished localization to the three-way junctions, suggesting that TMCC3 localized independently of binding to atlastins. TMCC3 knockdown caused a decrease in the number of three-way junctions and expansion of ER sheets, leading to a reduction of the tubular ER network in U2OS cells. The TMCC3 knockdown phenotype was partially rescued by the overexpression of atlastin-2, suggesting that TMCC3 knockdown would decrease the activity of atlastins. These results indicate that TMCC3 localizes at the three-way junctions for the proper tubular ER network.

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