Differential Regulation of Actin Depolymerizing Factor and Cofilin in Response to Alterations in the Actin Monomer Pool

Minamide, Laurie S.; Painter, W. B.; Schevzov, Galina; Gunning, Peter W.; Bamburg, James R.

doi:10.1074/jbc.272.13.8303

Cited by 45 publications

(31 citation statements)

References 67 publications

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“…Colocalization of ADF with monomeric actin is enhanced upon an increase in intracellular pH, whereas that of cofilin is less sensitive to pH changes (Bernstein et al, 2000), which is consistent with their in vitro properties (Yeoh et al, 2002). Expression of ADF, but not cofilin, is downregulated by an increase in the actin monomer pool (Minamide et al, 1997). In contrast, expression of cofilin, but not ADF, is upregulated in dystrophic muscles (Hayakawa et al, 1993;Nagaoka et al, 1996).…”

supporting

confidence: 54%

Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes inCaenorhabditis elegans

Ono

Parast

Alberico

et al. 2003

Journal of Cell Science

109

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Actin depolymerizing factor (ADF)/cofilin is an essential enhancer of actin turnover. Multicellular organisms express multiple ADF/cofilin isoforms in different patterns of tissue distribution. However, the functional significance of different ADF/cofilin isoforms is not understood. The Caenorhabditis elegans unc-60 gene generates two ADF/cofilins,UNC-60A and UNC-60B, by alternative splicing. These two ADF/cofilin proteins have different effects on actin dynamics in vitro, but their functional difference in vivo remains unclear. Here, we demonstrate that the two isoforms are expressed in different tissues and are required for distinct morphogenetic processes. UNC-60A was ubiquitously expressed in most embryonic cells and enriched in adult gonads, intestine and oocytes. In contrast, UNC-60B was specifically expressed in the body wall muscle, vulva and spermatheca. RNA interference of UNC-60A caused embryonic lethality with variable defects in cytokinesis and developmental patterning. In severely affected embryos, a cleavage furrow was formed and progressed but reversed before completion of the cleavage. Also, in some affected embryos, positioning of the blastomeres became abnormal, which resulted in embryonic arrest. In contrast, an unc-60B-null mutant was homozygous viable, underwent normal early embryogenesis and caused disorganization of actin filaments specifically in body wall muscle. These results suggest that the ADF/cofilin isoforms play distinct roles in specific aspects of actin reorganization in vivo.

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supporting

confidence: 54%

Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes inCaenorhabditis elegans

Ono

Parast

Alberico

et al. 2003

Journal of Cell Science

109

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“…19,[21][22][23][24] Increasing the monomeric actin pool in a murine myoblast cell line through expression of a mutant b-actin or with latrunculin A decreases ADF but not cofilin-1 expression, suggesting that their expression is differentially regulated within the same cell. 25 Cofilin-1 is usually considered ubiquitous whereas destrin expression seems specific of epithelia and endothelia, 19 suggesting that they may behave differently according to cell type and situations. Functional differences between these 2 proteins thus deserve investigation when both are expressed by a given cell type.…”

Section: Cancermentioning

confidence: 99%

Differential involvement of destrin and cofilin‐1 in the control of invasive properties of Isreco1 human colon cancer cells

Estornes

Gevrey

Navoizat

et al. 2007

Intl Journal of Cancer

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Actin depolymerizing factor (ADF)/cofilin family proteins are key regulators of actin filament turnover and cytoskeleton reorganization. The role of cofilin-1 in cell motility has been demonstrated in several cell types but remained poorly documented in the case of colon cancer. In addition, the putative function of destrin (also known as ADF) had not been explored in this context despite the fact that it is expressed in all colon cancer cell lines examined. We were therefore prompted to evaluate the respective contributions of these proteins to the invasive properties of the human colon cancer Isreco1 cell line, which expresses a comparatively high destrin/cofilin ratio. Reduction of cofilin-1 or destrin expression in Isreco1 cells using RNA interference led to an increase of the number of multinucleated cells and altered polarized lamellipodium protrusion and distribution of paxillin-containing adhesions. Both cofilin-1 and destrin silencing enhanced cell adhesion to extracellular matrix components. However, only destrin appeared to be required for cell migration on collagen I and for cell invasion through Matrigel in response to the proinvasive neuroendocrine peptide bombesin. This differential functional involvement was supported by a destrin-dependent, cofilin-independent phosphorylation of p130Crk-associated substrate (p130Cas) upon cell adhesion to collagen I or Matrigel. Taken together, our results suggest that destrin is a significant regulator of various processes important for invasive phenotype of human colon cancer Isreco1 cells whereas cofilin-1 may be involved in only a subset of them. ' 2007 Wiley-Liss, Inc.Key words: actin cytoskeleton; cofilin-1; destrin; invasion; colon cancerThe ability of colon tumor cells to invade adjacent structures and to metastasize at distant sites is the major cause of unfavorable outcome for colon cancer patients. However, the molecular mechanisms involved in these different steps remain largely unknown. Actin cytoskeletal reorganization is crucial for many different aspects of tumor progression, notably cell motility, cell adhesion, morphogenesis or cytokinesis, and is controlled to a great extent by the Rho family of GTPases (Rho, Rac and Cdc42).1,2 Remodeling of the actin cytoskeleton in response to extracellular stimuli acting through cell surface receptors is mediated by multiple actin-binding proteins that depolymerize/polymerize, nucleate, cap, sever or cross-link actin filaments. 3,4The actin depolymerizing factor (ADF)/cofilin family of proteins so far comprises 3 members: cofilin-1, a muscle-specific isoform cofilin-2 and destrin (another name of ADF in humans). These proteins are essential for enhancing the turnover rate of actin through their ability to sever actin filaments thereby creating new free barbed ends and to depolymerize filaments at their pointed ends (reviewed in 3, 5-7). ADF/cofilin proteins are mainly inactivated through phosphorylation on Ser3 by LIM kinase (LIMK) and TES kinase (TESK).8 Specific phosphatase slingshot (SSH) and chronophin ...

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“…Phosphorylation signals were quantified using Image Quant 5.0 software. Two-dimensional SDS-PAGE was performed as described (Minamide et al, 1997;Dong et al, 2001). The Pro35S:33 Flag-ADF4 construct was transformed into the wild type and ckl2 mutant, respectively.…”

Section: Kinase Activity Assaysmentioning

confidence: 99%

CASEIN KINASE1-LIKE PROTEIN2 Regulates Actin Filament Stability and Stomatal Closure via Phosphorylation of Actin Depolymerizing Factor

et al. 2016

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The opening and closing of stomata are crucial for plant photosynthesis and transpiration. Actin filaments undergo dynamic reorganization during stomatal closure, but the underlying mechanism for this cytoskeletal reorganization remains largely unclear. In this study, we identified and characterized Arabidopsis thaliana casein kinase 1-like protein 2 (CKL2), which responds to abscisic acid (ABA) treatment and participates in ABA-and drought-induced stomatal closure. Although CKL2 does not bind to actin filaments directly and has no effect on actin assembly in vitro, it colocalizes with and stabilizes actin filaments in guard cells. Further investigation revealed that CKL2 physically interacts with and phosphorylates actin depolymerizing factor 4 (ADF4) and inhibits its activity in actin filament disassembly. During ABA-induced stomatal closure, deletion of CKL2 in Arabidopsis alters actin reorganization in stomata and renders stomatal closure less sensitive to ABA, whereas deletion of ADF4 impairs the disassembly of actin filaments and causes stomatal closure to be more sensitive to ABA. Deletion of ADF4 in the ckl2 mutant partially recues its ABA-insensitive stomatal closure phenotype. Moreover, Arabidopsis ADFs from subclass I are targets of CKL2 in vitro. Thus, our results suggest that CKL2 regulates actin filament reorganization and stomatal closure mainly through phosphorylation of ADF.

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Differential Regulation of Actin Depolymerizing Factor and Cofilin in Response to Alterations in the Actin Monomer Pool

Cited by 45 publications

References 67 publications

Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes inCaenorhabditis elegans

Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes inCaenorhabditis elegans

Differential involvement of destrin and cofilin‐1 in the control of invasive properties of Isreco1 human colon cancer cells

CASEIN KINASE1-LIKE PROTEIN2 Regulates Actin Filament Stability and Stomatal Closure via Phosphorylation of Actin Depolymerizing Factor

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