Identification of a 14-3-3 Protein from<i>Lentinus edodes</i>That Interacts with CAP (Adenylyl Cyclase-associated Protein), and Conservation of This Interaction in Fission Yeast

Zhou, Guowei; Yamamoto, Takaharu; Ozoe, Fumiyo; Yano, Daisuke; Tanaka, Katsunori; Matsuda, Hideyuki; Kawamukai, Makoto

doi:10.1271/bbb.64.149

Cited by 25 publications

(12 citation statements)

References 45 publications

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“…In addition to S307/ S309, we also identified S36 as another phospho-regulatory site, although we have yet to identify the responsible kinase. Phosphoregulation may also be employed in fungal CAP, as we previously found that the N-terminal domain of CAP homologues from L. .edodes and S. pombe both interact with 14-3-3 protein homologues (Zhou et al, 2000), a family of chaperon proteins that bind phosphoproteins. We did not observe significant alterations in the morphology of cells that express CAP1 harboring mutations at the other phosphorylation sites that we found; however, we cannot exclude the possibility that they impact on other aspects of CAP1, such as subcellular localization.…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of the cytoskeletal protein CAP1 controls its association with cofilin and actin

Zhou

Zhang

et al. 2014

Journal of Cell Science

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Cell signaling can control the dynamic balance between filamentous and monomeric actin by modulating actin regulatory proteins. One family of actin regulating proteins that controls actin dynamics comprises cyclase-associated proteins 1 and 2 (CAP1 and 2, respectively). However, cell signals that regulate CAPs remained unknown. We mapped phosphorylation sites on mouse CAP1 and found S307 and S309 to be regulatory sites. We further identified glycogen synthase kinase 3 as a kinase phosphorylating S309. The phosphomimetic mutant S307D/S309D lost binding to its partner cofilin and, when expressed in cells, caused accumulation of actin stress fibers similar to that in cells with reduced CAP expression. In contrast, the non-phosphorylatable S307A/S309A mutant showed drastically increased cofilin binding and reduced binding to actin. These results suggest that the phosphorylation serves to facilitate release of cofilin for a subsequent cycle of actin filament severing. Moreover, our results suggest that S307 and S309 function in tandem; neither the alterations in binding cofilin and/or actin, nor the defects in rescuing the phenotype of the enlarged cell size in CAP1 knockdown cells was observed in point mutants of either S307 or S309. In summary, we identify a novel regulatory mechanism of CAP1 through phosphorylation.

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Section: Discussionmentioning

confidence: 99%

Phosphorylation of the cytoskeletal protein CAP1 controls its association with cofilin and actin

Zhou

Zhang

et al. 2014

Journal of Cell Science

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“…5) Cyr1 interacts with its associated protein Cap1, which plays a partly regulatory role of adenylyl cyclase and also interacts with actin and 14-3-3. [6][7][8] When cAMP is abundant, it associates with the regulatory subunit Cgs1, and the catalytic protein kinase Pka1 is released. 9) Pka1 phosphorylates in an inhibitory way the zinc-finger protein Rst2, which otherwise induces expression of ste11.…”

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confidence: 99%

Involvement of Moc1 in Sexual Development and Survival ofSchizosaccharomyces pombe

Yakura

Ishikura

Adachi

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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“…It functions as an adaptor that facilitates a diverse array of cellular processes by mediating specific protein interactions. In basidiomycetes Lentinula edodes, it was shown that 14-3-3 protein might play a role in regulation of adenylyl cyclase-associated protein (CAP) via physical interaction (Zhou et al, 2000). Vasara et al (2002) reported that 14-3-3 from the cellulase-producer Trichoderma reesei can interact with yeast secretory pathway components and the authors suggested that the 14-3-3 plays a role in protein secretion.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning of cDNAs for 14-3-3 and its protein interactions in a white-rot fungusPhanerochaete chrysosporium

Hong

Zhang

et al. 2006

Ann. Microbiol.

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The 14-3-3 is a highly conserved, ubiquitous expressed protein in eukaryotes and very important in the regulation of such crucial cellular processes as metabolism, signal transduction, cell-cycle control, apoptosis, protein trafficking, transcription, stress responses, and malignant transformation. In this study, the full-length cDNA of 14-3-3 was cloned first time from a white-rot fungus Phanerochaete chrysosporium. Yeast two hybrid has been performed to fish out the proteins that can bind with 14-3-3 in P. chrysosporium. The results showed that 14-3-3 could form homodimers in P. chrysosporium. Two novel proteins containing predicted WD domain could interact with 14-3-3, too. In addition, the transcription of 14-3-3 gene under low-nitrogen medium was constitutional by RT-PCR analysis. These results indicate that 14-3-3 protein in P. chrysosporium may be involved in multiple cellular processes.

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Identification of a 14-3-3 Protein fromLentinus edodesThat Interacts with CAP (Adenylyl Cyclase-associated Protein), and Conservation of This Interaction in Fission Yeast

Cited by 25 publications

References 45 publications

Phosphorylation of the cytoskeletal protein CAP1 controls its association with cofilin and actin

Phosphorylation of the cytoskeletal protein CAP1 controls its association with cofilin and actin

Involvement of Moc1 in Sexual Development and Survival ofSchizosaccharomyces pombe

Molecular cloning of cDNAs for 14-3-3 and its protein interactions in a white-rot fungusPhanerochaete chrysosporium

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