Linked Life Data

17202724

Source:http://linkedlifedata.com/resource/pubmed/id/17202724

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-3-26
pubmed:abstractText
Myo1, a heavy chain of type I myosin of the fission yeast Schizosaccharomyces pombe, is essential for sporulation. Here we have analyzed the expression, localization and cellular function of the type I myosin light chain calmodulin, Cam2, encoded by cam2(+). Transcription of cam2(+) was constitutive and markedly enhanced in meiosis. The cam2 null mutant was viable and completed sporulation normally at 28 degrees C, but formed four-spored asci poorly at 34 degrees C. In those sporulation-defective cells, the forespore membrane was formed abnormally. A Cam2-GFP fusion protein accumulated at the cell poles in interphase cells and at the medial septation site in postmitotic cells, colocalizing with Myo1 and F-actin patches. During the mating process, a single Cam2-GFP dot was detected at the tip of the mating projection. During meiosis-I, the Cam2-GFP dots dispersed into the cell periphery and the cytoplasm. At metaphase-II, intense Cam2-GFP signals appeared near Meu14 rings which were formed at the leading edge of expanding forespore membranes. This localization of Cam2 was dependent upon Myo1; and sporulation defect of cam2Delta at 34 degrees C was alleviated by overexpressing Myo1DeltaIQ. These results suggest a close relationship between Cam2 and Myo1. In addition, both F-actin and Myo1 localized with Cam2 in the leading edge region. In summary, type I myosin and F-actin accumulate at the leading edge area of the forespore membrane and may play a pivotal role in its assembly.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1347-3700
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
181-95
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Localization of type I myosin and F-actin to the leading edge region of the forespore membrane in Schizosaccharomyces pombe.
pubmed:affiliation
Department of Biology, Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't