The LIM Domains of WLIM1 Define a New Class of Actin Bundling Modules

Thomas, Clément; Moreau, Flora; Dieterle, Monika; Hoffmann, Céline; Gatti, Sabrina; Hofmann, Christina; Troys, Marleen Van; Ampè, Christophe; Steinmetz, André

doi:10.1074/jbc.m703691200

Cited by 39 publications

(57 citation statements)

References 48 publications

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“…Thus, by virtue of their distinct abilities, the two individual LIM domains and the linker region contribute differently to the two functions of WLIM1a. Consistent with our data, the LIM domain1 of tobacco WLIM1, was shown to be more efficient in actin bundling compared to the LIM domain2 of NtWLIM1 (Thomas et al, 2007), and both LIM domain1 and LIM domain2 of NtWLIM1 were found to be sufficient for the DNA binding activity of the protein (Kawaoka et al, 2000). It should be stressed that in our experiments, we furthermore observed that the actin-bundling activity of LIM domain1 and the PAL-box-binding activity of LIM domain2 were weaker than those of the native, non-truncated protein.…”

Section: Lim-domain Proteins Have Been Identified In Several Plantssupporting

confidence: 78%

“…Concerning LIM proteins, one assumption is that LIM domains could dimerize to fulfill their actin-bundling function (Thomas et al, 2007). Combined with our results, which suggest that both LIM domains directly bundle actin filaments (Figures 3 and 4) and truncated WLIM1a peptides are capable of forming dimers as verified by pull-down assay (Figure 6), we hypothesize that neighboring LIMs bundle actin filaments through dimerization.…”

Section: Lim-domain Proteins Have Been Identified In Several Plantssupporting

confidence: 68%

“…It has been reported that LIM proteins form dimers that facilitate actin bundling (Thomas et al, 2007). To assess if WLIM1a and its LIM domains can form dimers, we expressed GST-WLIM1a, GST-D1L, GST-LD2, GST-D1, GST-D2, and GST-L in E. coli.…”

Section: Wlim1a and Its Truncated Proteins Can Form Dimers In Solutionmentioning

confidence: 99%

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The two domains of cotton WLIM1a protein are functionally divergent

Han

Sun

et al. 2016

Sci. China Life Sci.

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Our previous study demonstrated that WLIM1a has dual roles in fiber elongation and secondary cell wall synthesis in upland cotton, and the protein acts either as an actin-binding protein or as a transcription factor. Because WLIM1a consists of two different LIM domains, it is possible that these elements contribute differentially to the dual functions of the protein. In this study, we dissected the two LIM domains and characterized their biochemical functions. By using red fluorescent protein (RFP) fusion, co-sedimentation, and DNA binding methods, we found that the two domains of WLIM1a, domain1 (D1) and domain2 (D2), possessed different biochemical properties. While D1 contributed primarily to the actin filament-bundling activity of WLIM1a, D2 contributed to the DNA-binding activity of the protein; both D1 and D2 relied on a linker sequence for their activities. In addition, we found that WLIM1a and its two LIM domains form dimers in vitro. These results may lead to a better understanding of the molecular mechanisms of dual functions of WLIM1a during cotton fiber development. WLIM1a, actin bundle, transcription factor, dual functionCitation:

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Section: Lim-domain Proteins Have Been Identified In Several Plantssupporting

confidence: 78%

Section: Lim-domain Proteins Have Been Identified In Several Plantssupporting

confidence: 68%

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The two domains of cotton WLIM1a protein are functionally divergent

Han

Sun

et al. 2016

Sci. China Life Sci.

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“…Regarding the mechanism underlying LIM proteinmediated actin bundling, each single LIM domain of NtWLIM1 is able to autonomously bundle AFs in vitro, although with a reduced efficiency compared to the fulllength, two-LIM domain containing, protein [Thomas et al, 2007]. From those data, two main models of bundling can be proposed (Fig.…”

Section: Lim Proteinsmentioning

confidence: 99%

Actin bundling in plants

Thomas

Tholl

Moes

et al. 2009

Cell Motil. Cytoskeleton

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Tight regulation of plant actin cytoskeleton organization and dynamics is crucial for numerous cellular processes including cell division, expansion and intracellular trafficking. Among the various actin regulatory proteins, actin-bundling proteins trigger the formation of bundles composed of several parallel actin filaments closely packed together. Actin bundles are present in virtually all plant cells, but their biological roles have rarely been addressed directly. However, decades of research in the plant cytoskeleton field yielded a bulk of data from which an overall picture of the functions supplied by actin bundles in plant cells emerges. Although plants lack several equivalents of animal actin-bundling proteins, they do possess major bundler classes including fimbrins, villins and formins. The existence of additional players is not excluded as exemplified by the recent characterization of plant LIM proteins, which trigger the formation of actin bundles both in vitro and in vivo. This apparent functional redundancy likely reflects the need for plant cells to engineer different types of bundles that act at different sub-cellular locations and exhibit specific function-related properties. By surveying information regarding the properties of plant actin bundles and their associated bundling proteins, the present review aims at clarifying why and how plants make actin bundles. Cell Motil. Cytoskeleton 66: 940-957, 2009. '

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“…Several classes of actin bundlers have been characterized in plants, including villins (7)(8)(9)(10)(11)(12), fimbrins (13,14), certain formins (15,16), and LIM proteins (17)(18)(19). These actin bundlers are also present in most other eukaryotes.…”

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confidence: 99%

Plant Actin-binding Protein SCAB1 Is Dimeric Actin Cross-linker with Atypical Pleckstrin Homology Domain

Zhang

Zhao

Guo

et al. 2012

Journal of Biological Chemistry

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Background: SCAB1 is a novel plant-specific actin-bundling protein.Results: SCAB1 consists of an actin-binding domain, two coiled-coil dimerization domains, and a fused immunoglobulin and pleckstrin homology domain with an atypical binding site for inositol phosphates. Conclusion: SCAB1 is a dimeric actin cross-linker and may be regulated by inositol signaling. Significance: This work provides a structural framework to understand the function of SCAB1.

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The LIM Domains of WLIM1 Define a New Class of Actin Bundling Modules

Cited by 39 publications

References 48 publications

The two domains of cotton WLIM1a protein are functionally divergent

The two domains of cotton WLIM1a protein are functionally divergent

Actin bundling in plants

Plant Actin-binding Protein SCAB1 Is Dimeric Actin Cross-linker with Atypical Pleckstrin Homology Domain

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