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PMID: 7490278 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Yeast Num1p associates with the mother cell cortex during S/G2 phase and affects microtubular functions.

The Journal of cell biology ·Vol. 131 ·No. 4 ·1995-11-00 ·Pages 1003-14

Farkasovsky M, Küntzel H

Abstract

The NUM1 gene is involved in the control of nuclear migration in Saccharomyces cerevisiae. The content of NUM1 mRNA fluctuates during the cell cycle, reaching a maximum at S/G2 phase, and the translation product Num1p associates with the cortex of mother cells mainly during S, G2, and mitosis, as seen by indirect immunofluorescence. The nuclear spindle in NUM1-deficient large-budded cells often fails to align along the mother/bud axis, while abnormally elongated astral microtubules emanate from both spindle pole bodies. A num1 null mutation confers temperature sensitivity to the cold-sensitive alpha-tubulin mutant tub1-1, and shows synthetic lethality with the beta-tubulin mutant alleles tub2-402, tub2-403, tub2-404, and tub2-405. Deletion mapping has defined three functionally important Num1p regions: a potential EF hand Ca2+ binding site, a cluster of potential phosphorylation sites and a pleckstrin homology domain. The latter domain appears to be involved in targeting Num1p to the mother cell cortex. Our data suggest that the periodically expressed NUM1 gene product controls nuclear migration by affecting astral microtubule functions.

MeSH Terms
Calcium-Binding Proteins/genetics,metabolism,ultrastructure Cell Membrane/metabolism Cell Nucleus/physiology Cytoskeletal Proteins Fluorescent Antibody Technique, Indirect Fungal Proteins/genetics,metabolism,ultrastructure G2 Phase/physiology Microscopy, Phase-Contrast Microtubules/physiology,ultrastructure Mutation/physiology Periodicity RNA, Messenger/metabolism S Phase/physiology Saccharomyces cerevisiae/genetics,metabolism Saccharomyces cerevisiae Proteins Spindle Apparatus/physiology Tubulin/genetics
Chemicals
Calcium-Binding Proteins Cytoskeletal Proteins Fungal Proteins NUM1 protein, S cerevisiae RNA, Messenger Saccharomyces cerevisiae Proteins Tubulin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Farkasovsky M
Max-Planck-Institut für experimentelle Medizin, Göttingen, Federal Republic of Germany.
Küntzel H
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
1995-11-00
Pages
1003-14
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2200000
Subset
IM
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