Mammalian Myosin-18A, a Highly Divergent Myosin

Guzik-Lendrum, Stephanie; Heissler, Sarah M.; Billington, Neil; Takagi, Yasuharu; Yang, Yi; Knight, Peter J.; Homsher, Earl; Sellers, James R.

doi:10.1074/jbc.m112.441238

Cited by 70 publications

(93 citation statements)

References 71 publications

(52 reference statements)

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“…The resulting phosphorylation of the non-muscle RLC2A (myosin-2A regulatory light chain) suggests an association of myosin-18A␣ with RLC2A. This hypothesis is supported by the fact that in vitro mouse myosin-18A binds essential and regulatory light chains via its neck region (4). The tripartite MRCK⅐LRAP35a⅐myosin-18A␣ complex localizes to lamellar actomyosin bundles, where non-muscle myosin-2A drives the retrograde flow (14,15).…”

mentioning

confidence: 48%

“…This interpretation is supported by the fact that both slow and fast rates for ATP and ADP binding are dependent on nucleotide concentration. The biphasic nucleotide binding behavior has not been observed for the mouse myosin-18A S1 construct (4). Also, the overall nucleotide affinities of human M18A-MD are about 30 times higher than for the mouse isoform, and the ADP-mediated switching to full binding ability has not been described before.…”

Section: Discussionmentioning

confidence: 73%

“…ADP is shown in a stick representation with black carbon atoms; the orange sphere designates the location of the Mg forms. Nevertheless, in their study, Guzik-Lendrum et al (4) utilized an S1 construct comprising a short N-terminal sequence preceding the motor domain and a neck region with bound essential and regulatory light chains. A previous study revealed differences for chicken skeletal muscle myosin S1 with wild-type versus truncated essential light chains in actin binding and ATPase activity, suggesting a direct interaction of the essential light chain N terminus with actin that is regulated by the SH3-like subdomain of myosin (39).…”

Section: Discussionmentioning

confidence: 99%

“…In a recent study, Drosophila myosin-18 has been found to be an actin-binding protein that does not bind nucleotide, has no ATPase activity, and cannot actively translocate over actin filaments (12). A current publication of the same group on functional features of mouse myosin-18A reports actin and nucleotide binding properties but no significant ATPase activity and suggests that this myosin is not a traditional motor (4). Moreover, the amino acid sequence of active site elements of the myosin-18 motor domain exhibits changes in highly conserved regions, which can prevent myosin-18 from productively interacting with ATP in the same way as other myosins.…”

mentioning

confidence: 99%

“…Like the founding member of this myosin class, MysPDZ (now termed mouse myosin-18A), human myosin-18A comprises a region rich in lysine and glutamate residues (KE) and a PDZ 3 module in its N-terminal extension. This domain is followed by a generic motor domain with an adjacent neck domain that can bind essential and regulatory light chains (4). The tail domain contains long stretches of coiled-coils that support heavy chain dimerization (5).…”

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confidence: 99%

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Functional Characterization of Human Myosin-18A and Its Interaction with F-actin and GOLPH3

Taft

Behrmann

Munske-Weidemann

et al. 2013

Journal of Biological Chemistry

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Background: Class-18A myosins share a unique N-terminal extension comprising a PDZ module and a KE-rich region. Results: Human myosin-18A binds F-actin via its motor domain in a nucleotide-dependent manner and via the KE-rich region, modulated by direct interaction between the PDZ module and GOLPH3. Conclusion: Myosin-18A binds F-actin and recruits interaction partners to the cytoskeleton. Significance: This work establishes a molecular basis for myosin-18A mediated membrane-cytoskeleton interplay.

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confidence: 48%

Section: Discussionmentioning

confidence: 73%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Functional Characterization of Human Myosin-18A and Its Interaction with F-actin and GOLPH3

Taft

Behrmann

Munske-Weidemann

et al. 2013

Journal of Biological Chemistry

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Four things to know about myosin light chains as reporters for non‐muscle myosin‐2 dynamics in live cells

Heissler

Sellers

2015

Cytoskeleton

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The interplay between nonmuscle myosins-2 and filamentous actin results in cytoplasmic contractility which is essential for eukaryotic life. Concomitantly, there is tremendous interest in elucidating the physiological function and temporal localization of nonmuscle myosin-2 in cells. A commonly used method to study the function and localization of nonmuscle myosin-2 is to overexpress a fluorescent protein (FP)-tagged version of the regulatory light chain (RLC) which binds to the myosin-2 heavy chain by mass action. Caveats about this approach include findings from recent studies indicating that the RLC does not bind exclusively to the nonmuscle myosin-2 heavy chain. Rather, it can also associate with the myosin heavy chains of several other classes as well as other targets than myosin. In addition, the presence of the FP moiety may compromise myosin’s enzymatic and mechanical performance. This and other factors to be discussed in this commentary raise questions about the possible complications in using FP-RLC as a marker for the dynamic localization and regulatory aspects of nonmuscle myosin-2 motor functions in cell biological experiments.

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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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Mammalian Myosin-18A, a Highly Divergent Myosin

Cited by 70 publications

References 71 publications

Functional Characterization of Human Myosin-18A and Its Interaction with F-actin and GOLPH3

Functional Characterization of Human Myosin-18A and Its Interaction with F-actin and GOLPH3

Four things to know about myosin light chains as reporters for non‐muscle myosin‐2 dynamics in live cells

Characterization of myosin II regulatory light chain isoforms in HeLa cells

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