UmTea1, a Kelch and BAR domain-containing protein, acts at the cell cortex to regulate cell morphogenesis in the dimorphic fungus Ustilago maydis

被引:7
|
作者
Woraratanadharm, Tad [1 ]
Kmosek, Stephanie [1 ]
Banuett, Flora [1 ]
机构
[1] Calif State Univ Long Beach, Dept Biol Sci, 1250 Bellflower Blvd, Long Beach, CA 90840 USA
基金
美国国家科学基金会;
关键词
Tea1 cell end marker; Cell polarity; Septum positioning; Cell and neck width; Ustilago maydis; Kelch domain protein; PLASMA-MEMBRANE DOMAINS; CORN SMUT FUNGUS; FISSION YEAST; POLARIZED GROWTH; FILAMENTOUS GROWTH; REPEAT SUPERFAMILY; CALCOFLUOR WHITE; HYPHAL GROWTH; FORMIN FOR3P; CYTOKINESIS;
D O I
10.1016/j.fgb.2018.09.002
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
The spatial organization of a cell is crucial for distribution of cell components and for cell morphogenesis in all organisms. Ustilago maydis, a basidiomycete fungus, has a yeast-like and a filamentous form. The former buds once per cell cycle at one of the cell poles, and can use the same site repeatedly or choose a new site at the same pole or opposite pole. The filamentous form consists of a long apical cell with short septate basal compartments lacking cytoplasm. It grows at the apex and can reverse growth forming a new growth zone at the basal end. We are interested in understanding how these different morphologies are generated. Here we present identification and characterization of U. maydis Tea1, a homologue of the fission yeast cell end marker Teal. We demonstrate that UmTea1, a Kelch domain protein, interacts with itself and is an important determinant of the site of polarized growth: teal mutants bud simultaneously from both cell poles and form bifurcate buds. UmTeal also regulates septum positioning, cell wall deposition, cell and neck width, coordination of nuclear division and cell separation, and localization of sterol-rich membrane domains. Some of these functions are shared with UmTea4, another cell end marker. We show that Teal::GFP localizes to sites of polarized or potential polarized growth and to the septation site in the yeast-like form. Additionally, localization of Tea1::GFP as rings along the filament suggests that the filament undergoes septation. We hypothesize that Teal may act as a scaffold for the assembly of proteins that determine the site of polarized growth.
引用
收藏
页码:10 / 28
页数:19
相关论文
共 50 条
  • [1] Fuz1, a MYND domain protein, is required for cell morphogenesis in Ustilago maydis
    Chew, Emily
    Aweiss, Yara
    Lu, Ching-Yu
    Banuett, Flora
    MYCOLOGIA, 2008, 100 (01) : 31 - 46
  • [2] Role of the nuclear migration protein Lis1 in cell morphogenesis in Ustilago maydis
    Valinluck, Michael
    Ahlgren, Sara
    Sawada, Mizuho
    Locken, Kristopher
    Banuett, Flora
    MYCOLOGIA, 2010, 102 (03) : 493 - 512
  • [3] Identification of Kel1p, a Kelch domain-containing protein involved in cell fusion and morphology in Saccharomyces cerevisiae
    Philips, J
    Herskowitz, I
    JOURNAL OF CELL BIOLOGY, 1998, 143 (02): : 375 - 389
  • [4] Characterization of Kelch domain-containing protein 7B in breast tumours and breast cancer cell lines
    Martin-Pardillos, Ana
    Ramon Y Cajal, Santiago
    ONCOLOGY LETTERS, 2019, 18 (03) : 2853 - 2860
  • [5] A kelch domain cell end protein, PoTea1, mediates cell polarization during appressorium morphogenesis in Pyricularia oryzae
    Qu, Yingmin
    Cao, Huijuan
    Huang, Pengyun
    Wang, Jing
    Liu, Xiaohong
    Lu, Jianping
    Lin, Fu-Cheng
    MICROBIOLOGICAL RESEARCH, 2022, 259
  • [6] Functional Role of Cell Surface CUB Domain-Containing Protein 1 in Tumor Cell Dissemination
    Deryugina, Elena I.
    Conn, Erin M.
    Wortmann, Andreas
    Partridge, Juneth J.
    Kupriyanova, Tatyana A.
    Ardi, Veronica C.
    Hooper, John D.
    Quigley, James P.
    MOLECULAR CANCER RESEARCH, 2009, 7 (08) : 1197 - 1211
  • [7] The formin homology domain-containing protein, FHOD1, enhances cell migration
    Westendorf, JJ
    DaCosta, K
    Neudauer, C
    McCarthy, JB
    Koka, S
    MOLECULAR BIOLOGY OF THE CELL, 2002, 13 : 46A - 46A
  • [8] Formin Homology Domain-Containing Protein 1 Regulates Smooth Muscle Cell Phenotype
    Staus, Dean P.
    Blaker, Alicia L.
    Medlin, Matt D.
    Taylor, Joan M.
    Mack, Christopher P.
    ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY, 2011, 31 (02) : 360 - U275
  • [9] The BAR Domain Protein PICK1 Regulates Cell Recognition and Morphogenesis by Interacting with Neph Proteins
    Hoehne, Martin
    Lorscheider, Johannes
    von Bardeleben, Anna
    Dufner, Matthias
    Scharf, M. Antonia
    Goedel, Markus
    Helmstaedter, Martin
    Schurek, Eva-Maria
    Zank, Sibylle
    Gerke, Peter
    Kurschat, Christine
    Sivritas, Sema Hayriye
    Neumann-Haefelin, Elke
    Huber, Tobias B.
    Reinhardt, H. Christian
    Schauss, Astrid C.
    Schermer, Bernhard
    Fischbach, Karl-Friedrich
    Benzing, Thomas
    MOLECULAR AND CELLULAR BIOLOGY, 2011, 31 (16) : 3241 - 3251
  • [10] The Tudor Domain-Containing Protein BbTdp1 Contributes to Fungal Cell Development, the Cell Cycle, Virulence, and Transcriptional Regulation in the Insect Pathogenic Fungus Beauveria bassiana
    Qiu, Lei
    Li, Ze
    Li Zhang
    Zhang, Tong-Sheng
    Hu, Shun-Juan
    Song, Ji-Zheng
    Liu, Jia-Hua
    Zhang, Jing
    Wang, Juan-Juan
    Cheng, Wen
    MICROBIOLOGY SPECTRUM, 2021, 9 (01): : 1 - 13