Faculty Opinions recommendation of Structure of a Ca2+-myristoyl switch protein that controls activation of a phosphatidylinositol 4-kinase in fission yeast.

2011 ◽  
Author(s):  
Wolfgang Jahnke
Keyword(s):  
Fission Yeast ◽  
Phosphatidylinositol 4 ◽  
Myristoyl Switch

scholarly journals Structure of a Ca2+-Myristoyl Switch Protein That Controls Activation of a Phosphatidylinositol 4-Kinase in Fission Yeast

2011 ◽  
Vol 286 (14) ◽  
pp. 12565-12577 ◽  
Author(s):  
Sunghyuk Lim ◽  
Thomas Strahl ◽  
Jeremy Thorner ◽  
James B. Ames
Keyword(s):  
Fission Yeast ◽  
Phosphatidylinositol 4 ◽  
Myristoyl Switch

scholarly journals Fission yeast myosin I facilitates PI(4,5)P2-mediated anchoring of cytoplasmic dynein to the cortex

2017 ◽  
Vol 114 (13) ◽  
pp. E2672-E2681 ◽  
Author(s):  
Jerrin Mathew Thankachan ◽  
Stephen Sukumar Nuthalapati ◽  
Nireekshit Addanki Tirumala ◽  
Vaishnavi Ananthanarayanan
Keyword(s):  
Fission Yeast ◽  
Total Internal Reflection ◽  
Nuclear Material ◽  
Cytoplasmic Dynein ◽  
Cell Cortex ◽  
Spindle Positioning ◽  
Binding Partner ◽  
Myosin I ◽  
Phosphatidylinositol 4

Several key processes in the cell, such as vesicle transport and spindle positioning, are mediated by the motor protein cytoplasmic dynein, which produces force on the microtubule. For the functions that require movement of the centrosome and the associated nuclear material, dynein needs to have a stable attachment at the cell cortex. In fission yeast, Mcp5 is the anchor protein of dynein and is required for the oscillations of the horsetail nucleus during meiotic prophase. Although the role of Mcp5 in anchoring dynein to the cortex has been identified, it is unknown how Mcp5 associates with the membrane as well as the importance of the underlying attachment to the nuclear oscillations. Here, we set out to quantify Mcp5 organization and identify the binding partner of Mcp5 at the membrane. We used confocal and total internal reflection fluorescence microscopy to count the number of Mcp5 foci and the number of Mcp5 molecules in an individual focus. Further, we quantified the localization pattern of Mcp5 in fission yeast zygotes and show by perturbation of phosphatidylinositol 4-phosphate 5-kinase that Mcp5 binds to phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2]. Remarkably, we discovered that the myosin I protein in fission yeast, Myo1, which is required for organization of sterol-rich domains in the cell membrane, facilitates the localization of Mcp5 and that of cytoplasmic dynein on the membrane. Finally, we demonstrate that Myo1-facilitated association of Mcp5 and dynein to the membrane determines the dynamics of nuclear oscillations and, in essence, dynein activity.

Mutation in fission yeast phosphatidylinositol 4-kinase Pik1 is synthetically lethal with defect in telomere protection protein Pot1

2018 ◽  
Vol 496 (4) ◽  
pp. 1284-1290 ◽  
Author(s):  
Asami Sugihara ◽  
Luan Cao Nguyen ◽  
Hossain Mohammad Shamim ◽  
Tetsushi Iida ◽  
Mai Nakase ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Telomere Protection ◽  
Synthetically Lethal ◽  
Phosphatidylinositol 4

scholarly journals A novel phosphatidylinositol(3,4,5)P3 pathway in fission yeast

2004 ◽  
Vol 166 (2) ◽  
pp. 205-211 ◽  
Author(s):  
Prasenjit Mitra ◽  
Yingjie Zhang ◽  
Lucia E. Rameh ◽  
Maria P. Ivshina ◽  
Dannel McCollum ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Mammalian Cells ◽  
Class I ◽  
Unexpected Finding ◽  
Class Iii ◽  
Growth And Survival ◽  
Higher Eukaryotes ◽  
Phosphoinositide 3 Kinase ◽  
Phosphatidylinositol 4 ◽  
Phosphatase And Tensin Homologue

The mammalian tumor suppressor, phosphatase and tensin homologue deleted on chromosome 10 (PTEN), inhibits cell growth and survival by dephosphorylating phosphatidylinositol-(3,4,5)-trisphosphate (PI[3,4,5]P3). We have found a homologue of PTEN in the fission yeast, Schizosaccharomyces pombe (ptn1). This was an unexpected finding because yeast (S. pombe and Saccharomyces cerevisiae) lack the class I phosphoinositide 3-kinases that generate PI(3,4,5)P3 in higher eukaryotes. Indeed, PI(3,4,5)P3 has not been detected in yeast. Surprisingly, upon deletion of ptn1 in S. pombe, PI(3,4,5)P3 became detectable at levels comparable to those in mammalian cells, indicating that a pathway exists for synthesis of this lipid and that the S. pombe ptn1, like mammalian PTEN, suppresses PI(3,4,5)P3 levels. By examining various mutants, we show that synthesis of PI(3,4,5)P3 in S. pombe requires the class III phosphoinositide 3-kinase, vps34p, and the phosphatidylinositol-4-phosphate 5-kinase, its3p, but does not require the phosphatidylinositol-3-phosphate 5-kinase, fab1p. These studies suggest that a pathway for PI(3,4,5)P3 synthesis downstream of a class III phosphoinositide 3-kinase evolved before the appearance of class I phosphoinositide 3-kinases.

scholarly journals Phosphatidylinositol 4-Phosphate 5-Kinase Its3 and Calcineurin Ppb1 Coordinately Regulate Cytokinesis in Fission Yeast

2000 ◽  
Vol 275 (45) ◽  
pp. 35600-35606 ◽  
Author(s):  
Yingjie Zhang ◽  
Reiko Sugiura ◽  
Yabin Lu ◽  
Masako Asami ◽  
Takuya Maeda ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Phosphatidylinositol 4

scholarly journals Immunocytochemical Localization and Crystal Structure of Human Frequenin (Neuronal Calcium Sensor 1)

2000 ◽  
Vol 276 (15) ◽  
pp. 11949-11955 ◽  
Author(s):  
Yves Bourne ◽  
Jens Dannenberg ◽  
Verena Pollmann ◽  
Pascale Marchot ◽  
Olaf Pongs
Keyword(s):  
Crystal Structure ◽  
Calcium Binding ◽  
Large Family ◽  
Synaptic Activity ◽  
Unknown Protein ◽  
Structural Differences ◽  
Ef Hands ◽  
Phosphatidylinositol 4 ◽  
Cellular Compartments ◽  
Myristoyl Switch

Frequenin, a member of a large family of myristoyl-switch calcium-binding proteins, functions as a calcium-ion sensor to modulate synaptic activity and secretion. We show that human frequenin colocalizes with ARF1 GTPase in COS-7 cells and occurs in similar cellular compartments as the phosphatidylinositol-4-OH kinase PI4Kβ, the mammalian homolog of the yeast kinase PIK1. In addition, the crystal structure of unmyristoylated, calcium-bound human frequenin has been determined and refined to 1.9 Å resolution. The overall fold of frequenin resembles those of neurocalcin and the photoreceptor, recoverin, of the same family, with two pairs of calcium-binding EF hands and three bound calcium ions. Despite the similarities, however, frequenin displays significant structural differences. A large conformational shift of the C-terminal region creates a wide hydrophobic crevice at the surface of frequenin. This crevice, which is unique to frequenin and distinct from the myristoyl-binding box of recoverin, may accommodate a yet unknown protein ligand.

scholarly journals First person – Chloe Snider

2020 ◽  
Vol 133 (23) ◽  
pp. jcs257246
Keyword(s):  
Plasma Membrane ◽  
Cell Division ◽  
Fission Yeast ◽  
Early Career ◽  
First Person ◽  
Early Career Researchers ◽  
Phosphatidylinositol 4 ◽  
Vanderbilt University ◽  
Selection Of

ABSTRACTFirst Person is a series of interviews with the first authors of a selection of papers published in Journal of Cell Science, helping early-career researchers promote themselves alongside their papers. Chloe Snider is first author on ‘Fission yeast Opy1 is an endogenous PI(4,5)P2 sensor that binds to the phosphatidylinositol 4-phosphate 5-kinase Its3’, published in JCS. Chloe is a PhD student in the lab of Kathleen Gould at Vanderbilt University, Nashville, TN, investigating how the cytokinetic ring is anchored to the plasma membrane during cell division.

scholarly journals A New Genetic Method for Isolating Functionally Interacting Genes: High plo1+-Dependent Mutants and Their Suppressors Define Genes in Mitotic and Septation Pathways in Fission Yeast

Genetics ◽  
2000 ◽  
Vol 155 (4) ◽  
pp. 1521-1534
Author(s):  
C Fiona Cullen ◽  
Karen M May ◽  
Iain M Hagan ◽  
David M Glover ◽  
Hiroyuki Ohkura
Keyword(s):  
Fission Yeast ◽  
Nuclear Division ◽  
High Dose ◽  
Truncated Form ◽  
Genetic Method ◽  
Multicopy Suppressors ◽  
Genes Encoding ◽  
Phosphatidylinositol 4 ◽  
Dose Dependent ◽  
Suppressor Analysis

Abstract We describe a general genetic method to identify genes encoding proteins that functionally interact with and/or are good candidates for downstream targets of a particular gene product. The screen identifies mutants whose growth depends on high levels of expression of that gene. We apply this to the plo1+ gene that encodes a fission yeast homologue of the polo-like kinases. plo1+ regulates both spindle formation and septation. We have isolated 17 high plo1+-dependent (pld) mutants that show defects in mitosis or septation. Three mutants show a mitotic arrest phenotype. Among the 14 pld mutants with septation defects, 12 mapped to known loci: cdc7, cdc15, cdc11 spg1, and sid2. One of the pld mutants, cdc7-PD1, was selected for suppressor analysis. As multicopy suppressors, we isolated four known genes involved in septation in fission yeast: spg1+, sce3+, cdc8+, and rho1+, and two previously uncharacterized genes, mpd1+ and mpd2+. mpd1+ exhibits high homology to phosphatidylinositol 4-phosphate 5-kinase, while mpd2+ resembles Saccharomyces cerevisiae SMY2; both proteins are involved in the regulation of actin-mediated processes. As chromosomal suppressors of cdc7-PD1, we isolated mutations of cdc16 that resulted in multiseptation without nuclear division. cdc16+, dma1+, byr3+, byr4+ and a truncated form of the cdc7 gene were isolated by complementation of one of these cdc16 mutations. These results demonstrate that screening for high dose-dependent mutants and their suppressors is an effective approach to identify functionally interacting genes.

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