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Phospholipase C-related catalytically inactive protein regulates cytokinesis by protecting phosphatidylinositol 4,5-bisphosphate from metabolism in the cleavage furrow.
Sci Rep 2019; 9(1):12729SR

Abstract

Cytokinesis is initiated by the formation and ingression of the cleavage furrow. Phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] accumulation followed by RhoA translocation to the cleavage furrow are prerequisites for cytokinesis progression. Here, we investigated whether phospholipase C (PLC)-related catalytically inactive protein (PRIP), a metabolic modulator of PI(4,5)P2, regulates PI(4,5)P2-mediated cytokinesis. We found that PRIP localised to the cleavage furrow during cytokinesis. Moreover, HeLa cells with silenced PRIP displayed abnormal cytokinesis. Importantly, PI(4,5)P2 accumulation at the cleavage furrow, as well as the localisation of RhoA and phospho-myosin II regulatory light chain to the cleavage furrow, were reduced in PRIP-silenced cells. The overexpression of oculocerebrorenal syndrome of Lowe-1 (OCRL1), a phosphatidylinositol-5-phosphatase, in cells decreased PI(4,5)P2 levels during early cytokinesis and resulted in cytokinesis abnormalities. However, these abnormal cytokinesis phenotypes were ameliorated by the co-expression of PRIP but not by co-expression of a PI(4,5)P2-unbound PRIP mutant. Collectively, our results indicate that PRIP is a component at the cleavage furrow that maintains PI(4,5)P2 metabolism and regulates RhoA-dependent progression of cytokinesis. Thus, we propose that PRIP regulates phosphoinositide metabolism correctively and mediates normal cytokinesis progression.

Authors+Show Affiliations

Department of Cellular and Molecular Pharmacology, Division of Basic Life Sciences, Institute of Biomedical and Health Sciences, Hiroshima University, 1-2-3, Kasumi, Minami-ku, Hiroshima, 734-8553, Japan.Department of Cellular and Molecular Pharmacology, Division of Basic Life Sciences, Institute of Biomedical and Health Sciences, Hiroshima University, 1-2-3, Kasumi, Minami-ku, Hiroshima, 734-8553, Japan.Department of Cellular and Molecular Pharmacology, Division of Basic Life Sciences, Institute of Biomedical and Health Sciences, Hiroshima University, 1-2-3, Kasumi, Minami-ku, Hiroshima, 734-8553, Japan.Department of Cellular and Molecular Pharmacology, Division of Basic Life Sciences, Institute of Biomedical and Health Sciences, Hiroshima University, 1-2-3, Kasumi, Minami-ku, Hiroshima, 734-8553, Japan.Department of Biological Science, Graduate School of Science, Hiroshima University, 1-3-1, Kagamiyama, Higashi-Hiroshima, Hiroshima, 739-8526, Japan.Division of Anatomy and Cell Biology, Faculty of Medicine, Tohoku Medical and Pharmaceutical University, 1-15-1, Fukumuro, Miyagino-ku, Sendai, Miyagi, 983-8536, Japan.Oral Medicine Research Center, Fukuoka Dental College, 2-15-1, Tamura, Sawara-ku, Fukuoka, 814-0193, Japan.Department of Cellular and Molecular Pharmacology, Division of Basic Life Sciences, Institute of Biomedical and Health Sciences, Hiroshima University, 1-2-3, Kasumi, Minami-ku, Hiroshima, 734-8553, Japan. taka-kanematsu@dent.kyushu-u.ac.jp. Department of Cell Biology and Pharmacology, Faculty of Dental Science, Kyushu University, 3-1-1, Maidashi, Higashi-ku, Fukuoka, 812-8582, Japan. taka-kanematsu@dent.kyushu-u.ac.jp.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31484968

Citation

Asano, Satoshi, et al. "Phospholipase C-related Catalytically Inactive Protein Regulates Cytokinesis By Protecting Phosphatidylinositol 4,5-bisphosphate From Metabolism in the Cleavage Furrow." Scientific Reports, vol. 9, no. 1, 2019, p. 12729.
Asano S, Ikura Y, Nishimoto M, et al. Phospholipase C-related catalytically inactive protein regulates cytokinesis by protecting phosphatidylinositol 4,5-bisphosphate from metabolism in the cleavage furrow. Sci Rep. 2019;9(1):12729.
Asano, S., Ikura, Y., Nishimoto, M., Yamawaki, Y., Hamao, K., Kamijo, K., ... Kanematsu, T. (2019). Phospholipase C-related catalytically inactive protein regulates cytokinesis by protecting phosphatidylinositol 4,5-bisphosphate from metabolism in the cleavage furrow. Scientific Reports, 9(1), p. 12729. doi:10.1038/s41598-019-49156-3.
Asano S, et al. Phospholipase C-related Catalytically Inactive Protein Regulates Cytokinesis By Protecting Phosphatidylinositol 4,5-bisphosphate From Metabolism in the Cleavage Furrow. Sci Rep. 2019 Sep 4;9(1):12729. PubMed PMID: 31484968.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Phospholipase C-related catalytically inactive protein regulates cytokinesis by protecting phosphatidylinositol 4,5-bisphosphate from metabolism in the cleavage furrow. AU - Asano,Satoshi, AU - Ikura,Yasuka, AU - Nishimoto,Mitsuki, AU - Yamawaki,Yosuke, AU - Hamao,Kozue, AU - Kamijo,Keiju, AU - Hirata,Masato, AU - Kanematsu,Takashi, Y1 - 2019/09/04/ PY - 2018/03/16/received PY - 2019/08/19/accepted PY - 2019/9/6/entrez PY - 2019/9/6/pubmed PY - 2019/9/6/medline SP - 12729 EP - 12729 JF - Scientific reports JO - Sci Rep VL - 9 IS - 1 N2 - Cytokinesis is initiated by the formation and ingression of the cleavage furrow. Phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] accumulation followed by RhoA translocation to the cleavage furrow are prerequisites for cytokinesis progression. Here, we investigated whether phospholipase C (PLC)-related catalytically inactive protein (PRIP), a metabolic modulator of PI(4,5)P2, regulates PI(4,5)P2-mediated cytokinesis. We found that PRIP localised to the cleavage furrow during cytokinesis. Moreover, HeLa cells with silenced PRIP displayed abnormal cytokinesis. Importantly, PI(4,5)P2 accumulation at the cleavage furrow, as well as the localisation of RhoA and phospho-myosin II regulatory light chain to the cleavage furrow, were reduced in PRIP-silenced cells. The overexpression of oculocerebrorenal syndrome of Lowe-1 (OCRL1), a phosphatidylinositol-5-phosphatase, in cells decreased PI(4,5)P2 levels during early cytokinesis and resulted in cytokinesis abnormalities. However, these abnormal cytokinesis phenotypes were ameliorated by the co-expression of PRIP but not by co-expression of a PI(4,5)P2-unbound PRIP mutant. Collectively, our results indicate that PRIP is a component at the cleavage furrow that maintains PI(4,5)P2 metabolism and regulates RhoA-dependent progression of cytokinesis. Thus, we propose that PRIP regulates phosphoinositide metabolism correctively and mediates normal cytokinesis progression. SN - 2045-2322 UR - https://www.unboundmedicine.com/medline/citation/31484968/Phospholipase_C-related_catalytically_inactive_protein_regulates_cytokinesis_by_protecting_phosphatidylinositol_4,5-bisphosphate_from_metabolism_in_the_cleavage_furrow L2 - http://dx.doi.org/10.1038/s41598-019-49156-3 DB - PRIME DP - Unbound Medicine ER -