Association of Elongation Factor 1α and Ribosomal Protein L3 with the Proline-Rich Region of Yeast Adenylyl Cyclase-Associated Protein CAP

Yanagihara, Chie; Shinkai, Masayuki; Kariya, Ken-ichi; Yamawaki-Kataoka, Yuriko; Hu, Chang‐Deng; Masuda, Tomomi; Kataoka, Tohru

doi:10.1006/bbrc.1997.6326

Cited by 13 publications

(9 citation statements)

References 29 publications

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“…Immunoblots indicated that Arp3 was efficiently eluted by PLP together with Abp1 (Supplemental Figure 1C). The interaction network is similar in yeast where Abp1 binds Myo5p and CAP/Srv2p via its SH3 domain (Freeman et al , 1996; Fazi et al , 2002) and the Arp2/3 complex via two acidic motifs (Goode et al , 2001), and CAP binds EF1α, RL3, and profilin (Yanagihara et al , 1997; Bertling et al , 2007). Demonstrating that Abp1 can bind the GPR domain in the context of MyoK full-length in vivo, Abp1 cofractionated with affinity-purified MyoK (Supplemental Figure 1D) and MyoK was coimmunoprecipitated with Abp1 (Figure 1E).…”

Section: Resultsmentioning

confidence: 99%

A Myosin IK-Abp1-PakB Circuit Acts as a Switch to Regulate Phagocytosis Efficiency

Dieckmann

Heyden

Kistler

et al. 2010

MBoC

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Section: Resultsmentioning

confidence: 99%

A Myosin IK-Abp1-PakB Circuit Acts as a Switch to Regulate Phagocytosis Efficiency

Dieckmann

Heyden

Kistler

et al. 2010

MBoC

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“…Construction of Expression Plasmids and Oligonucleotide-directed Mutagenesis-A plasmid, pAD-GST-CAP (18), was used to express the full-length CAP in yeast as a fusion protein with GST under control of the ADC1 promoter. Various deletions were introduced into the CAP gene by cleavage of pAD-GST-CAP with suitable pairs of restriction endonucleases and resealing by T4 DNA ligase with a linker oligonucleotide, 5Ј-CTAGTCTAGACTAG-3Ј, bearing stop codons in all reading frames, between.…”

Section: Methodsmentioning

confidence: 99%

“…The C-terminal function appears to be related to regulation of the actin cytoskeleton as evidenced by complementation of its defect by overexpression of profilin or SNC1 (13,14) and by demonstration of its direct association with actin monomer and of its actin-sequestering activity (15,16). In addition, CAP possesses two prolinerich sequences in its middle region intervening between the two regions, with which associations of actin-binding protein 1, elongation factor 1␣, and ribosomal protein L3 were recently shown (17,18).…”

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confidence: 99%

Coiled-coil Interaction of N-terminal 36 Residues of Cyclase-associated Protein with Adenylyl Cyclase Is Sufficient for Its Function in Saccharomyces cerevisiae Ras Pathway

Nishida

Shima

Sen

et al. 1998

Journal of Biological Chemistry

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In the budding yeast Saccharomyces cerevisiae, association with the 70-kDa cyclase-associated protein (CAP) is required for proper response of adenylyl cyclase to Ras proteins. We show here that a small segment comprising the N-terminal 36 amino acid residues of CAP is sufficient for association with adenylyl cyclase as well as for its function in the Ras-adenylyl cyclase pathway as assayed by the ability to confer RAS2Val-19 -dependent heat shock sensitivity to yeast cells. The CAPbinding site of adenylyl cyclase was mapped to a segment of 119 amino acid residues near its C terminus. Both of these regions contained tandem repetitions of a heptad motif ␣XX␣XXX (where ␣ represents a hydrophobic amino acid and X represents any amino acid), suggesting a coiled-coil interaction. When mutants of CAP defective in associating with adenylyl cyclase were isolated by screening of a pool of randomly mutagenized CAP, they were found to carry substitution mutations in one of the key hydrophobic residues in the heptad repeats. Furthermore, mutations of the key hydrophobic residues in the heptad repeats of adenylyl cyclase also resulted in loss of association with CAP. These results indicate the coiled-coil mechanism as a basis of the CAPadenylyl cyclase interaction.

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“…However, it remains to be determined whether this interaction affects the actin cable assembly-promoting activity of Bni1. Another reported ligand of Tef1 is the actin monomer-binding protein Srv2/CAP (see below) (417), but the in vitro and in vivo consequences of this interaction remain unknown.…”

Section: Organization and Stabilization Of Actin Filamentsmentioning

confidence: 99%

The Yeast Actin Cytoskeleton: from Cellular Function to Biochemical Mechanism

Moseley

Goode

2006

Microbiol Mol Biol Rev

362

427

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SUMMARY All cells undergo rapid remodeling of their actin networks to regulate such critical processes as endocytosis, cytokinesis, cell polarity, and cell morphogenesis. These events are driven by the coordinated activities of a set of 20 to 30 highly conserved actin-associated proteins, in addition to many cell-specific actin-associated proteins and numerous upstream signaling molecules. The combined activities of these factors control with exquisite precision the spatial and temporal assembly of actin structures and ensure dynamic turnover of actin structures such that cells can rapidly alter their cytoskeletons in response to internal and external cues. One of the most exciting principles to emerge from the last decade of research on actin is that the assembly of architecturally diverse actin structures is governed by highly conserved machinery and mechanisms. With this realization, it has become apparent that pioneering efforts in budding yeast have contributed substantially to defining the universal mechanisms regulating actin dynamics in eukaryotes. In this review, we first describe the filamentous actin structures found in Saccharomyces cerevisiae (patches, cables, and rings) and their physiological functions, and then we discuss in detail the specific roles of actin-associated proteins and their biochemical mechanisms of action.

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Association of Elongation Factor 1α and Ribosomal Protein L3 with the Proline-Rich Region of Yeast Adenylyl Cyclase-Associated Protein CAP

Cited by 13 publications

References 29 publications

A Myosin IK-Abp1-PakB Circuit Acts as a Switch to Regulate Phagocytosis Efficiency

A Myosin IK-Abp1-PakB Circuit Acts as a Switch to Regulate Phagocytosis Efficiency

Coiled-coil Interaction of N-terminal 36 Residues of Cyclase-associated Protein with Adenylyl Cyclase Is Sufficient for Its Function in Saccharomyces cerevisiae Ras Pathway

The Yeast Actin Cytoskeleton: from Cellular Function to Biochemical Mechanism

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