Actin-interacting Protein 1 Promotes Disassembly of Actin-depolymerizing Factor/Cofilin-bound Actin Filaments in a pH-dependent Manner

Nomura, Kazumi; Hayakawa, Kazuhide; Tatsumi, Hitoshi; Ono, Shoichiro

doi:10.1074/jbc.m115.713495

Cited by 22 publications

(17 citation statements)

References 63 publications

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“…In addition, another report shows that WDR1 might simply compete with Cofilin and dissociate redundant Cofilin from F-actin to accelerate severing activity (44). Furthermore, this regulation of Cofilin severing activity is dependent on the pH (46). In our study, we found WDR1 regulated Cofilin phosphorylation through LIMK1 to control the binding of Cofilin with actin filaments.…”

Section: Discussionsupporting

confidence: 52%

Trp-Asp (WD) Repeat Domain 1 Is Essential for Mouse Peri-implantation Development and Regulates Cofilin Phosphorylation

Xiao

Wan

et al. 2017

Journal of Biological Chemistry

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Edited by Xiao-Fan WangTrp-Asp (WD) repeat domain 1 (WDR1) is a highly conserved actin-binding protein across all eukaryotes and is involved in numerous actin-based processes by accelerating Cofilin severing actin filament. However, the function and the mechanism of WDR1 in mammalian early development are still largely unclear. We now report that WDR1 is essential for mouse periimplantation development and regulates Cofilin phosphorylation in mouse cells. The disruption of maternal WDR1 does not obviously affect ovulation and female fertility. However, depletion of zygotic WDR1 results in embryonic lethality at the periimplantation stage. In WDR1 knock-out cells, we found that WDR1 regulates Cofilin phosphorylation. Interestingly, WDR1 is overdosed to regulate Cofilin phosphorylation in mouse cells. Furthermore, we showed that WDR1 interacts with Lim domain kinase 1 (LIMK1), a well known phosphorylation kinase of Cofilin. Altogether, our results provide new insights into the role and mechanism of WDR1 in physiological conditions.The actin cytoskeleton is a highly dynamic structure that regulates cell motility, adhesion, division, and growth and has a fundamental function in embryonic development (1-3). In physiological conditions, actin filaments are continually assembled and disassembled in response to varied cellular activities (4, 5). The dynamics of F-actin is well orchestrated by a large number of actin-binding proteins (5, 6). Actin-depolymerizing factor Cofilin plays critical roles in the modulation of actin cytoskeleton dynamics (7). In vitro, Cofilin severs actin filament at low concentrations, whereas it fully decorates actin filaments and suppresses the severing activity at high concentrations (8, 9). In addition, Cofilin severing F-actin is not explained well for how the filaments of actin cytoskeleton can be rapidly disassembled in physiological conditions (4). Thus, the function of Cofilin in actin dynamics depends not only on its relative concentration to actin, but also on other regulatory proteins in vivo. Dysfunction of these regulating proteins results in aberrant actin cytoskeleton in various cellular and developmental processes (10 -12).Cofilin directly binds with actin to function as a regulator of the actin dynamics (13). However, the phosphorylation of Cofilin at Ser-3 blocks its binding site to actin (14, 15). Thus, the activity of Cofilin is controlled by phosphorylation and dephosphorylation processes, which are regulated by cascade reactions of several protein kinases and phosphatases. Lim domain kinases (LIMKs) 4 and testis-specific protein kinases (TESKs) are responsible for the phosphorylation of Cofilin, whereas slingshot (SSH) family protein phosphatases and pyridoxal phosphatase (PDXP) catalyze the dephosphorylation reaction (16 -20). These kinases and phosphatases are also regulated by their phosphorylation or localization in cytoplasm to maintain the level of Cofilin phosphorylation in response to extracellular stimuli (21-23).The activity of Cofilin on actin disassembly is gr...

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Section: Discussionsupporting

confidence: 52%

Trp-Asp (WD) Repeat Domain 1 Is Essential for Mouse Peri-implantation Development and Regulates Cofilin Phosphorylation

Xiao

Wan

et al. 2017

Journal of Biological Chemistry

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“…The binding of cofilin to cortactin is one of the mechanisms of cofilin inactivation which is typical for podosomes and invadopodia, actin-based dynamic protrusions produced by invasive cancer cells, vascular cells, and macrophages [ 124 , 125 ]. Actin-interacting protein 1 (AIP1) and cyclase-associated protein 1 (CAP1) promote the disassembly of cofilin-bound actin filaments [ 126 , 127 ]. Coronin provides recruiting cofilin to filament sides and thus enhances actin filament severing [ 128 ].…”

Section: Actin-depolymerizing Factor/cofilin Superfamilymentioning

confidence: 99%

Cofilin-1 and Other ADF/Cofilin Superfamily Members in Human Malignant Cells

Shishkin

Eremina

Pashintseva

et al. 2016

IJMS

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Identification of actin-depolymerizing factor homology (ADF-H) domains in the structures of several related proteins led first to the formation of the ADF/cofilin family, which then expanded to the ADF/cofilin superfamily. This superfamily includes the well-studied cofilin-1 (Cfl-1) and about a dozen different human proteins that interact directly or indirectly with the actin cytoskeleton, provide its remodeling, and alter cell motility. According to some data, Cfl-1 is contained in various human malignant cells (HMCs) and is involved in the formation of malignant properties, including invasiveness, metastatic potential, and resistance to chemotherapeutic drugs. The presence of other ADF/cofilin superfamily proteins in HMCs and their involvement in the regulation of cell motility were discovered with the use of various OMICS technologies. In our review, we discuss the results of the study of Cfl-1 and other ADF/cofilin superfamily proteins, which may be of interest for solving different problems of molecular oncology, as well as for the prospects of further investigations of these proteins in HMCs.

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“…WD40 has important roles in histone recognition, chromatin function, RNA processing and transcriptional regulation (Suganuma et al, 2008). WD repeat domain-containing proteins, such as AIP1, disassemble the actin filaments decorated with ADF and shorten the ADF-severed actin filaments, thus maintaining a high concentration of cellular actin monomers (Nomura et al, 2016). The adenylyl cyclase-associated protein (OsACP) is highly implicated in positive regulation of actin turnover process (Ono, 2013) as an actin-sequestering protein.…”

Section: Discussionmentioning

confidence: 99%

An actin‐depolymerizing factor from the halophyte smooth cordgrass, Spartina alterniflora (SaADF2), is superior to its rice homolog (OsADF2) in conferring drought and salt tolerance when constitutively overexpressed in rice

Sengupta

Mangu

Sanchez

et al. 2018

Plant Biotechnology Journal

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Summary Actin‐depolymerizing factors ( ADF s) maintain the cellular actin network dynamics by regulating severing and disassembly of actin filaments in response to environmental cues. An ADF isolated from a monocot halophyte, Spartina alterniflora ( Sa ADF 2 ), imparted significantly higher level of drought and salinity tolerance when expressed in rice than its rice homologue Os ADF 2 . Sa ADF 2 differs from Os ADF 2 by a few amino acid residues, including a substitution in the regulatory phosphorylation site serine‐6, which accounted for its weak interaction with Os CDPK 6 (calcium‐dependent protein kinase), thus resulting in an increased efficacy of Sa ADF 2 and enhanced cellular actin dynamics. Sa ADF 2 overexpression preserved the actin filament organization better in rice protoplasts under desiccation stress. The predicted tertiary structure of Sa ADF 2 showed a longer F‐loop than Os ADF 2 that could have contributed to higher actin‐binding affinity and rapid F‐actin depolymerization in vitro by Sa ADF 2. Rice transgenics constitutively overexpressing Sa ADF 2 ( Sa ADF 2 ‐ OE ) showed better growth, relative water content, and photosynthetic and agronomic yield under drought conditions than wild‐type ( WT ) and Os ADF 2 overexpressers ( Os ADF 2‐ OE ). Sa ADF 2 ‐ OE preserved intact grana structure after prolonged drought stress, whereas WT and Os ADF 2 ‐ OE presented highly damaged and disorganized grana stacking. The possible role of ADF 2 in transactivation was hypothesized from the comparative transcriptome analyses, which showed significant differential expression of stress‐related genes including interacting partners of ADF 2 in overexpressers. Identification of a complex, differential interactome decorating or regulating stress‐modulated cytoskeleton driven by ADF isoforms will lead us to key pathways that could be potential target for genome engineering to improve abiotic stress tolerance in agricultural crops.

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Actin-interacting Protein 1 Promotes Disassembly of Actin-depolymerizing Factor/Cofilin-bound Actin Filaments in a pH-dependent Manner

Cited by 22 publications

References 63 publications

Trp-Asp (WD) Repeat Domain 1 Is Essential for Mouse Peri-implantation Development and Regulates Cofilin Phosphorylation

Trp-Asp (WD) Repeat Domain 1 Is Essential for Mouse Peri-implantation Development and Regulates Cofilin Phosphorylation

Cofilin-1 and Other ADF/Cofilin Superfamily Members in Human Malignant Cells

An actin‐depolymerizing factor from the halophyte smooth cordgrass, Spartina alterniflora (SaADF2), is superior to its rice homolog (OsADF2) in conferring drought and salt tolerance when constitutively overexpressed in rice

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