Phosphorylation of myosin II regulatory light chain by ZIP kinase is responsible for cleavage furrow ingression during cell division in mammalian cultured cells

Hosoba, Kosuke; Komatsu, Setsuko; Ikebe, Mitsuo; Kotani, Manato; Wenqin, Xiao; Tachibana, Taro; Hosoya, Hiroshi; Hamao, Kozue

doi:10.1016/j.bbrc.2015.03.005

Cited by 10 publications

(7 citation statements)

References 38 publications

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“…Therefore, we examined whether the MRLC isoforms actually served as kinase substrates because MRLC phosphorylation causes myosin II activation [Ikebe and Hartshorne, ; Ikebe, ]. Each purified MRLC was incubated with human ZIP‐kinase, which is known to be a representative kinase for MRLC at Thr18/Ser19 [Murata‐Hori et al, 1999, 2001; Hosoba et al, ]. As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Characterization of myosin II regulatory light chain isoforms in HeLa cells

et al. 2015

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Myosin II regulatory light chain (MRLC) is canonically known as a subunit of conventional myosin (myosin II), which tunes cytoplasmic contractility in cells. Recent studies have also revealed the noncanonical functions of MRLC, such as engagement with other proteins including unconventional myosins. Three MRLC isoforms (MRLC1, MRLC2, and MRLC3) are known in humans. The characteristics of MRLC2 are well known, but those of MRLC1 and MRLC3 are unclear; therefore, the properties of the three MRLC isoforms were investigated. The MRLCs were all phosphorylated at Thr18/Ser19, which is required for myosin II stimulation. MRLC mRNAs were expressed at the same level throughout the cell cycle in HeLa cells. The MRLCs colocalized with each other and their turnover rate was similar to that of myosin II heavy chain. Depletion of all the MRLCs perturbed cell spreading. The overproduction of MRLC2 or MRLC3, but not MRLC1, could effectively compensate for this defect, suggesting that MRLC2 and MRLC3 play dominant roles in cell spreading. Finally, computer simulations of the three-dimensional protein structures indicated that the location of the N-terminus of MRLC1 differs from that of MRLC2 or MRLC3, depending on its sequence. Thus, these MRLC isoforms have overlapping but distinct functions have been proposed.

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Section: Resultsmentioning

confidence: 99%

Characterization of myosin II regulatory light chain isoforms in HeLa cells

et al. 2015

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“…Additionally, a reduction in focal adhesion kinase (FAK) activity by the ectopic expression of DAPK3 (Nehru et al, 2013) may contribute to cell adhesion regulation during epithelial wound repair with impacts on IEC proliferation and survival (Owen et al, 2011). The augmentation of MLC20 phosphorylation by DAPK3 stimulates actomyosin contraction and cleavage furrow ingression (Hosoba et al, 2015), which are important for cytokinesis during cell division (Ono et al, 2020). Finally, the presence of a loss-of-function DAPK3 mutant Asp161Asn was associated with cytokinesis failure and could induce multinucleation via decreased actomyosin phosphorylation at the contractile ring in CRC cells (Ono et al, 2020).…”

Section: Potential For Dapk3 Involvement In Epithelial Wound Repairmentioning

confidence: 99%

Death‐associated protein kinases and intestinal epithelial homeostasis

Chen

MacDonald

2022

The Anatomical Record

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“…Previous studies have reported that death-associated protein kinase 3 (DAPK3), also known as ZIPK, directly phosphorylates MYL9 and regulates the actomyosin contraction in vascular smooth muscle via MYL9 phosphorylation [15,16]. In addition, recent studies have shown that DAPK3 also regulates cleavage furrow ingression in cytokinesis [17][18][19].…”

Section: Introductionmentioning

confidence: 99%

Leucine zipper protein 1 (LUZP1) regulates the constriction velocity of the contractile ring during cytokinesis

Hyodo,

Asano‐Inami,

Ito

et al. 2023

The FEBS Journal

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There has been a great deal of research on cell division and its mechanisms; however, its processes still have many unknowns. To find novel proteins that regulate cell division, we performed the screening using siRNAs and/or the expression plasmid of the target genes and identified leucine zipper protein 1 (LUZP1). Recent studies have shown that LUZP1 interacts with various proteins and stabilizes the actin cytoskeleton; however, the function of LUZP1 in mitosis is not known. In this study, we found that LUZP1 colocalized with the chromosomal passenger complex (CPC) at the centromere in metaphase and at the central spindle in anaphase and that these LUZP1 localizations were regulated by CPC activity and kinesin family member 20A (KIF20A). Mass spectrometry analysis identified that LUZP1 interacted with death‐associated protein kinase 3 (DAPK3), one regulator of the cleavage furrow ingression in cytokinesis. In addition, we found that LUZP1 also interacted with myosin light chain 9 (MYL9), a substrate of DAPK3, and comprehensively inhibited MYL9 phosphorylation by DAPK3. In line with a known role for MYL9 in the actin‐myosin contraction, LUZP1 suppression accelerated the constriction velocity at the division plane in our time‐lapse analysis. Our study indicates that LUZP1 is a novel regulator for cytokinesis that regulates the constriction velocity of the contractile ring.

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Phosphorylation of myosin II regulatory light chain by ZIP kinase is responsible for cleavage furrow ingression during cell division in mammalian cultured cells

Cited by 10 publications

References 38 publications

Characterization of myosin II regulatory light chain isoforms in HeLa cells

Characterization of myosin II regulatory light chain isoforms in HeLa cells

Death‐associated protein kinases and intestinal epithelial homeostasis

Leucine zipper protein 1 (LUZP1) regulates the constriction velocity of the contractile ring during cytokinesis

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