Identification and Phylogenetic Analysis of Drosophila melanogaster Myosins

Tzolovsky, George; Millo, Hadas; Pathirana, Stephen; Wood, Timothy; Bownes, Mary

doi:10.1093/oxfordjournals.molbev.a004163

Cited by 36 publications

(43 citation statements)

References 52 publications

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“…The fruit fly Drosophila melanogaster features 13 myosins, of which 12 belong to eight previously described classes, whereas one myosin (Myo29D, GenBank accession no. AAF52683) has so far been unclassified (20). Our analyses show that this myosin belongs to a so far insect-specific myosin class XX that is well supported (100% BS, Fig.…”

Section: Resultssupporting

confidence: 65%

New insights into myosin evolution and classification

Foth

Goedecke

Soldati

2006

Proc. Natl. Acad. Sci. U.S.A.

435

436

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Myosins are eukaryotic actin-dependent molecular motors important for a broad range of functions like muscle contraction, vision, hearing, cell motility, and host cell invasion of apicomplexan parasites. Myosin heavy chains consist of distinct head, neck, and tail domains and have previously been categorized into 18 different classes based on phylogenetic analysis of their conserved heads. Here we describe a comprehensive phylogenetic examination of many previously unclassified myosins, with particular emphasis on sequences from apicomplexan and other chromalveolate protists including the model organism Toxoplasma, the malaria parasite Plasmodium, and the ciliate Tetrahymena. Using different phylogenetic inference methods and taking protein domain architectures, specific amino acid polymorphisms, and organismal distribution into account, we demonstrate a hitherto unrecognized common origin for ciliate and apicomplexan class XIV myosins. Our data also suggest common origins for some apicomplexan myosins and class VI, for classes II and XVIII, for classes XII and XV, and for some microsporidian myosins and class V, thereby reconciling evolutionary history and myosin structure in several cases and corroborating the common coevolution of myosin head, neck, and tail domains. Six novel myosin classes are established to accommodate sequences from chordate metazoans (class XIX), insects (class XX), kinetoplastids (class XXI), and apicomplexans and diatom algae (classes XXII, XXIII, and XXIV). These myosin (sub)-classes include sequences with protein domains (FYVE, WW, UBA, ATS1-like, and WD40) previously unknown to be associated with myosin motors. Regarding the apicomplexan ''myosome,'' we significantly update class XIV classification, propose a systematic naming convention, and discuss possible functions in these parasites.Apicomplexa ͉ Chromalveolata

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Section: Resultssupporting

confidence: 65%

New insights into myosin evolution and classification

Foth

Goedecke

Soldati

2006

Proc. Natl. Acad. Sci. U.S.A.

435

436

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“…Besides Myo31DF, two other Myosin I family proteins have been identified in the Drosophila melanogaster genome, Myo61F, and Myosin95E (Myo95E). 15,16,22 Given the role of Myo31DF in the development of LR asymmetry in Drosophila, we expected that Myo61F and Myo95E were also probably involved in it. Especially, these two Myosin proteins may be required for developing reversed laterality in Myo31DF mutant embryos.…”

Section: Fly E2mentioning

confidence: 99%

Roles of Type I Myosins in Drosophila Handedness

Taniguchi¹,

Hozumi²,

Maeda³

et al. 2007

Fly

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“…Even so, these multiple class I myosins are predicted to have overlapping functions, as found in yeast and Dictyostelium (Tyska et al 2005;Nambiar et al 2009;Chen et al 2012), complicating the understanding of their in vivo roles (Kim and Flavell 2008). Thus, the knockout and analysis of multiple class I myosin genes in vertebrates would represent a major challenge.Three class I myosin genes, Myo31DF, Myo61F, and Myo95E have been identified in Drosophila ( Figure 1A) (Tzolovsky et al 2002). Myo31DF and Myo61F are closely …”

mentioning

confidence: 97%

“…Three class I myosin genes, Myo31DF, Myo61F, and Myo95E have been identified in Drosophila ( Figure 1A) (Tzolovsky et al 2002). Myo31DF and Myo61F are closely …”

mentioning

confidence: 97%

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Class I Myosins Have Overlapping and Specialized Functions in Left-Right Asymmetric Development inDrosophila

et al. 2015

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The class I myosin genes are conserved in diverse organisms, and their gene products are involved in actin dynamics, endocytosis, and signal transduction. Drosophila melanogaster has three class I myosin genes, Myosin 31DF (Myo31DF), Myosin 61F (Myo61F), and Myosin 95E (Myo95E). Myo31DF, Myo61F, and Myo95E belong to the Myosin ID, Myosin IC, and Myosin IB families, respectively. Previous loss-of-function analyses of Myo31DF and Myo61F revealed important roles in left-right (LR) asymmetric development and enterocyte maintenance, respectively. However, it was difficult to elucidate their roles in vivo, because of potential redundant activities. Here we generated class I myosin double and triple mutants to address this issue. We found that the triple mutant was viable and fertile, indicating that all three class I myosins were dispensable for survival. A loss-of-function analysis revealed further that Myo31DF and Myo61F, but not Myo95E, had redundant functions in promoting the dextral LR asymmetric development of the male genitalia. Myo61F overexpression is known to antagonize the dextral activity of Myo31DF in various Drosophila organs. Thus, the LR-reversing activity of overexpressed Myo61F may not reflect its physiological function. The endogenous activity of Myo61F in promoting dextral LR asymmetric development was observed in the male genitalia, but not the embryonic gut, another LR asymmetric organ. Thus, Myo61F and Myo31DF, but not Myo95E, play tissue-specific, redundant roles in LR asymmetric development. Our studies also revealed differential colocalization of the class I myosins with filamentous (F)-actin in the brush border of intestinal enterocytes.KEYWORDS myosin I; Myosin 31DF; Myosin 61F; Myosin 95E; left-right asymmetry T HE class I myosin genes encode myosin heavy chains, which are conserved in phylogenetically diverse organisms (Sellers 2000;Krendel and Mooseker 2005). The class I myosins are nonfilamentous, actin-based motor proteins and were the first discovered unconventional myosin proteins. These myosins are involved in a variety of cellular processes, such as cell migration, cell adhesion, and cell growth, through their regulation of actin dynamics, endocytosis, and signal transduction (Osherov and May 2000;Krendel and Mooseker 2005;Kim and Flavell 2008;McConnell and Tyska 2010).The structure of the myosin I heavy chains is evolutionarily conserved and composed of head (or motor), neck, and tail domains ( Figure 1A) (Coluccio 1997;Barylko et al. 2000). The head domain binds to filamentous (F)-actin and adenosine triphosphate (ATP), a common feature of myosin proteins ( Figure 1A) (Mermall et al. 1998); the neck domain possesses one or more IQ motifs, which directly interact with calmodulin or calmodulin-related myosin light chains (Coluccio 1997;Barylko et al. 2000), and the tail domains are divided into short and long types. Short tails contain a single tail homology 1 (TH1) domain, which is rich in basic residues and thought to interact with plasma membranes (Coluccio 1997;Barylko...

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Identification and Phylogenetic Analysis of Drosophila melanogaster Myosins

Cited by 36 publications

References 52 publications

New insights into myosin evolution and classification

New insights into myosin evolution and classification

Roles of Type I Myosins in Drosophila Handedness

Class I Myosins Have Overlapping and Specialized Functions in Left-Right Asymmetric Development inDrosophila

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