Imp2, the PSTPIP homolog in fission yeast, affects sensitivity to the immunosuppressant FK506 and membrane trafficking in fission yeast.
Imp2, the PSTPIP homolog in fission yeast, affects sensitivity to the immunosuppressant FK506 and membrane trafficking in fission yeast.
复制标题
Imp2 是裂殖酵母中的 PSTPIP 同源物,影响裂殖酵母中对免疫抑制剂 FK506 的敏感性和膜运输。
DOI:
10.1016/j.bbrc.2014.12.100
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发表时间:
2015
期刊:
影响因子:
--
通讯作者:
Reiko Sugiura
中科院分区:
文献类型:
--
作者:
Ayako Kita;Mari Higa;Akira Doi;Ryosuke Satoh;Reiko Sugiura
Cytokinesis is a highly ordered process that divides one cell into two cells, which is functionally linked to the dynamic remodeling of the plasma membrane coordinately with various events such as membrane trafficking. Calcineurin is a highly conserved serine/threonine protein phosphatase, which regulates multiple biological functions, such as membrane trafficking and cytokinesis. Here, we isolatedimp2-c3, a mutant allele of theimp2+gene, encoding a homolog of the mouse PSTPIP1 (proline-serine-threoninephosphataseinteractingprotein1), using a genetic screen for mutations that are synthetically lethal with calcineurin deletion in fission yeast. Theimp2-c3mutants showed a defect in cytokinesis with multi-septated phenotypes, which was further enhanced upon treatment with the calcineurin inhibitor FK506. Notably, electron micrographs revealed that theimp2-c3mutant cells accumulated aberrant multi-lamella Golgi structures and putative post-Golgi secretory vesicles, and exhibited fragmented vacuoles in addition to thickened septa. Consistently,imp2-c3mutants showed a reduced secretion of acid phosphatase and defects in vacuole fusion. Theimp2-c3mutant cells exhibited a weakened cell wall, similar to the membrane trafficking mutants identified in the same genetic screen such asypt3-i5. These findings implicate the PSTPIP1 homolog Imp2 in Golgi/vacuole function, thereby affecting various cellular processes, including cytokinesis and cell integrity.