A lasp family protein of Ciona intestinalis

Terasaki, Asako G.; Hiruta, Jin; Suzuki, Junko; Sakamoto, Shinya; Nishioka, Tatsuji; Suzuki, Hiroshi; Ohashi, Kazuyo; Azumi, Kaoru; Ogasawara, Michio

doi:10.1016/j.bbagrm.2007.08.001

Cited by 8 publications

(21 citation statements)

References 35 publications

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“…It has been reported that various invertebrates have genes encoding proteins homologous to vertebrate lasps [16]. Of these invertebrate lasps, the recombinant ascidian lasp molecule is indeed able to bind to F-actin in vitro [16]. The LIM domain and first nebulin-repeat of ascidian lasp showed high similarity to those of vertebrates, but other nebulin-repeats and linker sequences showed less homology.…”

Section: Discussionmentioning

confidence: 99%

“…Considering this previous report and the marked homology between lasp-1 and -2 in the LIM domain and n1 regions (93.7% and 85.7%, respectively) (Figure 5), these regions may be conserved for F-actin binding in both molecules. It has been reported that various invertebrates have genes encoding proteins homologous to vertebrate lasps [16]. Of these invertebrate lasps, the recombinant ascidian lasp molecule is indeed able to bind to F-actin in vitro [16].…”

Section: Discussionmentioning

confidence: 99%

“…Although lasp-1 is a LASP1 gene product in mammals and aves, lasp-2 is a splicing variant from the LASP2/NEBL gene, which concurrently encodes nebulette, an actin-binding protein expressed specifically in cardiac muscle [14], [15]. The mRNA of vertebrate lasp-2 is constituted from seven exons of the LASP2/NEBL gene [14], [16]. Both lasp-1 and lasp-2 bind to F-actin in vitro and colocalize at filopodial actin bundles and focal adhesions in several established cell lines [8], [10], [11], [17].…”

Section: Introductionmentioning

confidence: 99%

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Contribution of the LIM Domain and Nebulin-Repeats to the Interaction of Lasp-2 with Actin Filaments and Focal Adhesions

et al. 2009

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Lasp-2 binds to actin filaments and concentrates in the actin bundles of filopodia and lamellipodia in neural cells and focal adhesions in fibroblastic cells. Lasp-2 has three structural regions: a LIM domain, a nebulin-repeat region, and an SH3 domain; however, the region(s) responsible for its interactions with actin filaments and focal adhesions are still unclear. In this study, we revealed that the N-terminal fragment from the LIM domain to the first nebulin-repeat module (LIM-n1) retained actin-binding activity and showed a similar subcellular localization to full-length lasp-2 in neural cells. The LIM domain fragment did not interact with actin filaments or localize to actin filament bundles. In contrast, LIM-n1 showed a clear subcellular localization to filopodial actin bundles. Although truncation of the LIM domain caused the loss of F-actin binding activity and the accumulation of filopodial actin bundles, these truncated fragments localized to focal adhesions. These results suggest that lasp-2 interactions with actin filaments are mediated through the cooperation of the LIM domain and the first nebulin-repeat module in vitro and in vivo. Actin filament binding activity may be a major contributor to the subcellular localization of lasp-2 to filopodia but is not crucial for lasp-2 recruitment to focal adhesions.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Contribution of the LIM Domain and Nebulin-Repeats to the Interaction of Lasp-2 with Actin Filaments and Focal Adhesions

et al. 2009

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“…Although the bulk of the research on nebulin proteins has been in vertebrates, genes of the nebulin family can also be found in invertebrates [8-10]. Genomic analyses suggest that the number of nebulin family members has increased over the course of evolution.…”

Section: Structure and Evolution Of The Nebulin Family: How To Becomementioning

confidence: 99%

“…Genomic analyses suggest that the number of nebulin family members has increased over the course of evolution. Non-chordate invertebrates such as nematodes, fruit flies and sea urchins only have lasp-like genes, which contain a LIM domain, 2-3 nebulin repeats and an SH3 domain [8, 10]. However, the chordate invertebrate lancelet only contains a single huge nebulin-like gene.…”

Section: Structure and Evolution Of The Nebulin Family: How To Becomementioning

confidence: 99%

The Nebulin family: an actin support group

Pappas¹,

Bliss²,

Zieseniß³

et al. 2011

Trends in Cell Biology

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Nebulin, a giant actin-binding protein, is the largest member of a family of proteins (including N-RAP, nebulette, lasp-1 and lasp-2) which are assembled in a variety of cytoskeletal structures and expressed in different tissues. For decades nebulin has been thought to act as a molecular ruler, specifying the precise length of actin filaments in skeletal muscle. However, emerging evidence suggests that nebulin should not be viewed as a ruler but as an actin filament stabilizer required for length maintenance. Nebulin has also recently been implicated in an array of regulatory functions independent of its role in actin filament length regulation. In this review, we discuss the current evolutionary, biochemical, and functional data for the nebulin family of proteins -a family whose members, both large and small, function as cytoskeletal scaffolds and stabilizers.

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The emergence of nebulin repeats and evolution of lasp family proteins

et al. 2021

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The LIM and SH3 domain protein (lasp) family, the smallest proteins in the nebulin superfamily, consists of vertebrate lasp‐1 expressed in various non‐muscle tissues, vertebrate lasp‐2 expressed in the brain and cardiac muscle, and invertebrate lasp whose functions have been analyzed in Ascidiacea and Insecta. Gene evolution of the lasp family proteins was investigated by multiple alignments, comparison of gene structure, and synteny analyses in eukaryotes in which mRNA expression was confirmed. All invertebrates analyzed in this study belonging to the clade Filasterea, with the exception of Placozoa, have at least one lasp gene. The minimal actin‐binding region (LIM domain and first nebulin repeat) and SH3 domain detected in vertebrate lasp‐2 were found to be conserved among the lasp family proteins, and we showed that nematode lasp has actin‐binding activity. The linker sequences vary among invertebrate lasp proteins, implying that the lasp family proteins have universal and diverse functions. Gene structures and syntenic analyses suggest that a gene fragment encoding two nebulin repeats and a linker emerged in Filasterea or Holozoa, and the first lasp gene was generated following combination of three gene fragments encoding the LIM domain, two nebulin repeats with a linker, and the SH3 domain.

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A lasp family protein of Ciona intestinalis

Cited by 8 publications

References 35 publications

Contribution of the LIM Domain and Nebulin-Repeats to the Interaction of Lasp-2 with Actin Filaments and Focal Adhesions

Contribution of the LIM Domain and Nebulin-Repeats to the Interaction of Lasp-2 with Actin Filaments and Focal Adhesions

The Nebulin family: an actin support group

The emergence of nebulin repeats and evolution of lasp family proteins

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