<i>Arabidopsis</i>LIM Proteins: A Family of Actin Bundlers with Distinct Expression Patterns and Modes of Regulation

Papuga, Jessica; Hoffmann, Céline; Dieterle, Monika; Moes, Danièle; Moreau, Flora; Tholl, Stéphane; Steinmetz, André; Thomas, Clément

doi:10.1105/tpc.110.075960

Cited by 97 publications

(158 citation statements)

References 83 publications

(122 reference statements)

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“…The LIMs represent a distinct protein family with actin-binding domain unrelated to ABD2 (31). Although LIMs exhibited relatively high levels of diffuse cytoplasmic fluorescence compared with that of ABD2-GFP, cells expressing these GFP-LIMs showed AF organization and dynamic patterns in response to Bgh penetration similar to those in ABD2-GFP-expressing cells (Fig.…”

Section: Resultsmentioning

confidence: 89%

Myosins XI modulate host cellular responses and penetration resistance to fungal pathogens

Yang

Qin

Liu

et al. 2014

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

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The rapid reorganization and polarization of actin filaments (AFs) toward the pathogen penetration site is one of the earliest cellular responses, yet the regulatory mechanism of AF dynamics is poorly understood. Using live-cell imaging in Arabidopsis, we show that polarization coupled with AF bundling involves precise spatiotemporal control at the site of attempted penetration by the nonadapted barley powdery mildew fungus, Blumeria graminis f. sp. hordei (Bgh). We further show that the Bgh-triggered AF mobility and organelle aggregation are predominately driven by the myosin motor proteins. Inactivation of myosins by pharmacological inhibitors prevents bulk aggregation of organelles and blocks recruitment of lignin-like compounds to the penetration site and deposition of callose and defensive protein, PENETRATION 1 (PEN1) into the apoplastic papillae, resulting in attenuation of penetration resistance. Using gene knockout analysis, we demonstrate that highly expressed myosins XI, especially myosin XI-K, are the primary contributors to cell wall-mediated penetration resistance. Moreover, the quadruple myosin knockout mutant xi-1 xi-2 xi-i xi-k displays impaired trafficking pathway responsible for the accumulation of PEN1 at the cell periphery. Strikingly, this mutant shows not only increased penetration rate but also enhanced overall disease susceptibility to both adapted and nonadapted fungal pathogens. Our findings establish myosins XI as key regulators of plant antifungal immunity.actin cytoskeleton | plant immunity | endocytosis | vesicle | endocytic trafficking

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Section: Resultsmentioning

confidence: 89%

Myosins XI modulate host cellular responses and penetration resistance to fungal pathogens

Yang

Qin

Liu

et al. 2014

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

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“…Sequence alignment ( Figure 1B) shows that WLIM1a shares high sequence similarity with other plant LIM-domain proteins such as AtWLIM1, AtPLIM2c (Papuga et al, 2010), LlLIM1 (Wang et al, 2008), Ntlim1 (Kawaoka et al, 2000), and NtWLIM1 (Thomas et al, 2006). Interestingly, the two LIM domains of WLIM1a only share 40% amino acid sequence identity although both contain a 56-amino acid LIM motif ( Figure 1C).…”

Section: Wlim1a Contains Two Lim Domains With Low Sequence Similaritymentioning

confidence: 98%

“…In Arabidopsis, all six LIM-domain proteins were found to decorate actin filaments (Papuga et al, 2010). In tobacco, NtWLIM1 and NtWLIM2 were found to be both actin binding/bundling proteins and transcriptional regulators that activate the expression of prxC2 and histone, respectively (Kawaoka and Ebinuma, 2001;Moes et al, 2013).…”

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

confidence: 99%

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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“…The research on LIM proteins in the last few decades has also expanded its functional relevance outside animal kingdom and demonstrates role in fungal pathogenicity, plant immunity, pollen, fibre development, etc. (Papuga et al 2010;Han et al 2013;Li et al 2014;Xu et al 2015). In this way, the functions of these proteins are now taking shape into many biological prospects relevant to crop improvement.…”

Section: Introductionmentioning

confidence: 99%

The plant LIM proteins: unlocking the hidden attractions

Srivastava

Verma

2017

Planta

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Main conclusion The plant LIMs comprise two subfamilies with one (DA1/DAR) and two (2LIM) LIM domains. This review comprehensively discussed the structure and potential role of this protein family in diverse area of plant biology.The description of first eukaryote lineage-specific plant LIM domain (LIN11, ISL1, and MEC3) proteins was observed in Helianthus long back. The successive study of LIM proteins in diverse plants has shown its vital relation to development, metabolism and defence. This nascent gene family has been worked out for their role in actin dynamics, organ size determination and transcription regulation. On grounds of protein architecture, two sub-families have been delineated as DA1/DAR (one LIM domain) and 2LIMs (two LIM domains). The genomic and expression study guides to the identification of diverse subcategories. The significance of 2LIMs in regulation of actin dynamics leading to pollen growth and development has prospects to understand the plant reproductive behaviour. Interestingly, new facet of these LIMs as a transcriptional regulator in biological pathway/biosynthesis was also reported. Recently, the cumulative contribution of these features was also recognized for obtaining good quality fibre, thus giving translational outlook to this family. The DA1/DAR proteins are orchestrated with additional domains and provide a key role in regulation of organ size and tolerance to biotic and abiotic stress. This review will focus the journey of plant LIMs till date and will cover details of its structure, type, classification and functional relevance. This will provide insight to identify the potential of this gene family in the improvement of desired crop features.

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ArabidopsisLIM Proteins: A Family of Actin Bundlers with Distinct Expression Patterns and Modes of Regulation

Cited by 97 publications

References 83 publications

Myosins XI modulate host cellular responses and penetration resistance to fungal pathogens

Myosins XI modulate host cellular responses and penetration resistance to fungal pathogens

The two domains of cotton WLIM1a protein are functionally divergent

The plant LIM proteins: unlocking the hidden attractions

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