Sarcomeric actin organization is synergistically promoted by tropomodulin, ADF/cofilin, AIP1 and profilin in <i>C. elegans</i>

Yamashiro, Sawako; Cox, Elisabeth A.; Baillie, David L.; Hardin, Jeff; Ono, Shoichiro

doi:10.1242/jcs.040477

Cited by 35 publications

(54 citation statements)

References 58 publications

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“…Ono et al, 1994;Vartiainen et al, 2002;Bertling et al, 2004;Yamashiro et al, 2008). This led us to examine the turnover of actin filaments in neonatal cardiomyocytes, which display regular sarcomeric actin arrays and undergo spontaneous beating (= contractility) in cell culture conditions.…”

Section: Discussionmentioning

confidence: 99%

Contractility-dependent actin dynamics in cardiomyocyte sarcomeres

Skwarek‐Maruszewska

Hotulainen

Mattila

et al. 2009

Journal of Cell Science

100

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are required to disassemble non-productive filaments in developing cardiomyocytes. These data indicate that an excess of actin filaments is produced during sarcomere assembly, and that contractility is applied to recognize non-productive filaments that are subsequently destined for depolymerization. Consequently, contractility-induced actin dynamics plays an important role in sarcomere maturation. Supplementary material available online at

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Section: Discussionmentioning

confidence: 99%

Contractility-dependent actin dynamics in cardiomyocyte sarcomeres

Skwarek‐Maruszewska

Hotulainen

Mattila

et al. 2009

Journal of Cell Science

100

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“…6 A; Table 1). Similarly, unc94/tmd-1 loss of function alleles in C. elegans and morpholino knockdown of Tmod4 in developing X. laevis skeletal muscle result in aberrant myofibril assembly and defective movement (15,79,80).…”

Section: Tmods Regulate Thin Filament Lengths By Capping Pointed Endsmentioning

confidence: 99%

Tropomodulins and Leiomodins: Actin Pointed End Caps and Nucleators in Muscles

Fowler

Domínguez

2017

Biophysical Journal

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Cytoskeletal structures characterized by actin filaments with uniform lengths, including the thin filaments of striated muscles and the spectrin-based membrane skeleton, use barbed and pointed-end capping proteins to control subunit addition/dissociation at filament ends. While several proteins cap the barbed end, tropomodulins (Tmods), a family of four closely related isoforms in vertebrates, are the only proteins known to specifically cap the pointed end. Tmods are $350 amino acids in length, and comprise alternating tropomyosin-and actin-binding sites (TMBS1, ABS1, TMBS2, and ABS2). Leiomodins (Lmods) are related in sequence to Tmods, but display important differences, including most notably the lack of TMBS2 and the presence of a C-terminal extension featuring a proline-rich domain and an actin-binding WASP-Homology 2 domain. The Lmod subfamily comprises three somewhat divergent isoforms expressed predominantly in muscle cells. Biochemically, Lmods differ from Tmods, acting as powerful nucleators of actin polymerization, not capping proteins. Structurally, Lmods and Tmods display crucial differences that correlate well with their different biochemical activities. Physiologically, loss of Lmods in striated muscle results in cardiomyopathy or nemaline myopathy, whereas complete loss of Tmods leads to failure of myofibril assembly and developmental defects. Yet, interpretation of some of the in vivo data has led to the idea that Tmods and Lmods are interchangeable or, at best, different variants of two subfamilies of pointed-end capping proteins. Here, we review and contrast the existing literature on Tmods and Lmods, and propose a model of Lmod function that attempts to reconcile the in vitro and in vivo data, whereby Lmods nucleate actin filaments that are subsequently capped by Tmods during sarcomere assembly, turnover, and repair.

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“…Thymosin β 10 and Tmod1 have been identified as interacting proteins in a yeast two-hybrid screen, and the binding region on Tmod1 has been mapped to residues 162 -230 (86) . Tmod capping of the pointed end of actin filaments inhibited the actin depolymerization activity of ADF/cofilin in in vitro experiments (87) . Tms have also been shown to control the access of ADF/cofilin to actin filaments in an isoform-specific manner (88) .…”

Section: Interactions Of Tmods-tms With Other Actinassociated Proteinsmentioning

confidence: 93%

Tropomodulins and tropomyosins – organizers of cellular microcompartments

Fath

2013

BioMolecular Concepts

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Eukaryotic cells show a remarkable compartmentalization into compartments such as the cell nucleus, the Golgi apparatus, the endoplasmic reticulum, and endosomes. However, organelle structures are not the only means by which specialized compartments are formed. Recent research shows a critical role for diverse actin filament populations in defining functional compartments, here referred to as microcompartments, in a wide range of cells. These microcompartments are involved in regulating fundamental cellular functions including cell motility, plasma membrane organization, and cellular morphogenesis. In this overview, the importance of two multigene families of actin-associated proteins, tropomodulins and tropomyosins, their interactions with each other, and a large number of other proteins will be discussed in the context of generating specialized actin-based microcompartments.

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Sarcomeric actin organization is synergistically promoted by tropomodulin, ADF/cofilin, AIP1 and profilin in C. elegans

Cited by 35 publications

References 58 publications

Contractility-dependent actin dynamics in cardiomyocyte sarcomeres

Contractility-dependent actin dynamics in cardiomyocyte sarcomeres

Tropomodulins and Leiomodins: Actin Pointed End Caps and Nucleators in Muscles

Tropomodulins and tropomyosins – organizers of cellular microcompartments

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