Identification and functional analysis of the essential and regulatory light chains of the only type II myosin Myo1p in <i>Saccharomyces cerevisiae </i>

Luo, Juan; Vallen, Elizabeth A.; Dravis, Christopher; Tcheperegine, Serguei E.; Drees, Becky; Bi, Erfei

doi:10.1083/jcb.200401040

Cited by 62 publications

(121 citation statements)

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“…2), and its localization to the division site depends on its binding to Myo1 [Luo et al, 2004]. Cells deleted for MLC2 do not exhibit defects in actin ring formation but display a mild defect in Myo1 disassembly during and/or toward the end of cytokinesis [Luo et al, 2004]. As described above, Mlc1 is the ELC for Myo1 but its binding to the IQ motif of Myo1 is not required for AMR assembly [Luo et al, 2004].…”

Section: Amr Assemblymentioning

confidence: 99%

“…It displays an identical localization pattern to that of Myo1 throughout the cell cycle (Fig. 2), and its localization to the division site depends on its binding to Myo1 [Luo et al, 2004]. Cells deleted for MLC2 do not exhibit defects in actin ring formation but display a mild defect in Myo1 disassembly during and/or toward the end of cytokinesis [Luo et al, 2004].…”

Section: Amr Assemblymentioning

confidence: 99%

“…Mlc2 is the sole regulatory light chain (RLC) for Myo1 [Luo et al, 2004]. It displays an identical localization pattern to that of Myo1 throughout the cell cycle (Fig.…”

Section: Amr Assemblymentioning

confidence: 99%

“…Cells deleted for MLC2 do not exhibit defects in actin ring formation but display a mild defect in Myo1 disassembly during and/or toward the end of cytokinesis [Luo et al, 2004]. As described above, Mlc1 is the ELC for Myo1 but its binding to the IQ motif of Myo1 is not required for AMR assembly [Luo et al, 2004]. Mlc1 is also a light chain for Myo2 [Stevens and Davis, 1998], a myosin-V in budding yeast that plays an essential role in vesicle and organelle transport [Bretscher, 2003], but cells expressing Myo2 that lacks the Mlc1-binding site are still able to assemble an actin ring [Wloka and Bi, unpublished data].…”

Section: Amr Assemblymentioning

confidence: 99%

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Mechanisms of cytokinesis in budding yeast

Wloka

2012

Cytoskeleton

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Cytokinesis is essential for cell proliferation in all domains of life. Because the core components and mechanisms of cytokinesis are conserved from fungi to humans, the budding yeast Saccharomyces cerevisiae has served as an attractive model for studying this fundamental process. Cytokinesis in budding yeast is driven by two interdependent cellular events: actomyosin ring (AMR) constriction and the formation of a chitinous cell wall structure called the primary septum (PS), the functional equivalent of extracellular matrix remodeling during animal cytokinesis. AMR constriction is thought to drive efficient plasma membrane ingression as well as to guide PS formation, whereas PS formation is thought to stabilize the AMR during its constriction. Following the completion of the PS formation, two secondary septa (SS), consisting of glucans and mannoproteins, are synthesized at both sides of the PS. Degradation of the PS and a part of the SS by a chitinase and glucanases then enables cell separation. In this review, we discuss the mechanics of cytokinesis in budding yeast, highlighting its common and unique features as well as the emerging questions. © 2012 Wiley Periodicals, Inc.

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Section: Amr Assemblymentioning

confidence: 99%

Section: Amr Assemblymentioning

confidence: 99%

“…Mlc2 is the sole regulatory light chain (RLC) for Myo1 [Luo et al, 2004]. It displays an identical localization pattern to that of Myo1 throughout the cell cycle (Fig.…”

Section: Amr Assemblymentioning

confidence: 99%

Section: Amr Assemblymentioning

confidence: 99%

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Mechanisms of cytokinesis in budding yeast

Wloka

2012

Cytoskeleton

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“…Phosphorylation of MRLC2 has been proposed as an efficient regulatory mechanism in the crossbridge cycle, calcium sensitivity, and other parameters strengthening muscle performance (Sweeney et al, 1993;Reddy et al, 2002). Phosphorylation of MRLC2 is likely crucial for generating force in non-muscle cells and smooth muscle cells (Murata-Hori et al, 2000;Luo et al, 2004). Previous studies have shown that phosphorylation of MRLC at Ser19 and Thr18 enhances the actin-activated Mg-ATPase activity of myosin II and promotes the assembly of myosin II filaments in vitro (Ikebe, 1989).…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning and functional analysis of MRLC2 in Tianfu, Boer, and Chengdu Ma goats

Xu¹,

Xu²,

Lu³

et al. 2013

Genet. Mol. Res.

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ABSTRACT.To determine the molecular basis of heterosis in goats, fluorescence quantitative polymerase chain reaction (PCR) was performed to investigate myosin-regulatory light chain 2 (MRLC2) gene expression in the longissimus dorsi muscle tissues of the Tianfu goat and its parents, the Boer and Chengdu Ma goats. The goat MRLC2 gene was differentially expressed in the crossbreed, and the purebred mRNA were isolated and identified using fluorescence quantitative reverse transcription-PCR (RT-PCR). The complete coding sequence of MRLC2 was obtained using the cDNA method, and the full-length coding sequence consisted of 513 bp encoding 172 amino acids. The EF-hand superfamily domain of the MRLC2 protein is well conserved in caprine and other animals. The deduced amino acid sequence of MRLC2 shared significant identity with MRLC2 from other mammals. Phylogenetic tree analysis revealed that the MRLC2 protein was closely related to MRLC2 in other mammals. Several predicted miRNA target sites were found in the coding sequence of caprine MRLC2 mRNA. Analysis by RT-PCR showed that MRLC2 mRNA was present in the ©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 12 (3): 3510-3520 (2013) Function analysis of the MRLC2 gene 3511 heart, stomach, liver, spleen, lung, small intestine, kidney, leg muscle, abdominal muscle, and longissimus dorsi muscles. In particular, the high expression of MRLC2 mRNA was detected in the longissimus dorsi, leg muscle, abdominal muscle, stomach, and heart, but low levels of expression were also observed in the liver, spleen, lung, small intestine, and kidney. The expression of the MRLC2 gene was upregulated in the longissimus dorsi muscle of Boer and Tianfu goats, and it was moderately upregulated in Chengdu Ma goats.

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Native nonmuscle myosin II stability and light chain binding in Drosophila melanogaster

Franke

Boury

Gerald

et al. 2006

Cell Motil. Cytoskeleton

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Native nonmuscle myosin IIs play essential roles in cellular and developmental processes throughout phylogeny. Individual motor molecules consist of a heterohexameric complex of three polypeptides which, when properly assembled, are capable of force generation. Here, we more completely characterize the properties, relationships and associations that each subunit has with one another in Drosophila melanogaster. All three native nonmuscle myosin II polypeptide subunits are expressed in close to constant stoichiometry to each other throughout development. We find that the stability of two subunits, the heavy chain and the regulatory light chain, depend on one another whereas the stability of the third subunit, the essential light chain, does not depend on either the heavy chain or regulatory light chain. We demonstrate that heavy chain aggregates, which form when regulatory light chain is lacking, associate with the essential light chain in vivo-thus showing that regulatory light chain association is required for heavy chain solubility. By immunodepletion we find that the majority of both light chains are associated with the nonmuscle myosin II heavy chain but pools of free light chain and/or light chain bound to other proteins are present. We identify four myosins (myosin II, myosin V, myosin VI and myosin VIIA) and a microtubule-associated protein (asp/Abnormal spindle) as binding partners for the essential light chain (but not the regulatory light chain) through mass spectrometry and co-precipitation. Using an in silico approach we identify six previously uncharacterized genes that contain IQ-motifs and may be essential light chain binding partners.

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Identification and functional analysis of the essential and regulatory light chains of the only type II myosin Myo1p in Saccharomyces cerevisiae

Cited by 62 publications

References 51 publications

Mechanisms of cytokinesis in budding yeast

Mechanisms of cytokinesis in budding yeast

Molecular cloning and functional analysis of MRLC2 in Tianfu, Boer, and Chengdu Ma goats

Native nonmuscle myosin II stability and light chain binding in Drosophila melanogaster

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