ACTIN: General Principles from Studies in Yeast
Annual Review of Cell and Developmental BiologyPublished 1 November 1996
Kathryn R. Ayscough, David G. Drubin
Citations59
SJR quartileQ1
SJR score6.79
SNIP2.74
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TL;DR
Advances in general understanding of actin properties, interactions with other proteins, and regulation of the actin cytoskeleton, derived from studies in the budding yeast S. cerevisiae are highlighted.
Abstract
Three of the most important questions concerning actin function are: (a) How does actin structure relate to actin function? (b) How does each of the numerous proteins that interact with actin contribute to actin cytoskeleton function in vivo? (c) How are the activities of these proteins regulated? Powerful molecular genetics combined with well-established biochemical techniques make the yeast Saccharomyces cerevisiae an ideal organism for studies aimed at answering these questions. The protein sequences and biochemical properties of actin and its interacting proteins and the pathways that regulate these interactions all appear to be conserved, indicating that principles elucidated from studies in yeast will apply to all eukaryotes. In this review, we highlight advances in our general understanding of actin properties, interactions with other proteins, and regulation of the actin cytoskeleton, derived from studies in the budding yeast S. cerevisiae.
Keywords
MedicineBiochemistry, Genetics and Molecular Biology
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131 Citations1994Brian K. Haarer, A. Petzold +2 more
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Journal of Biological ChemistryFurther characterization of a conserved actin-binding 27-kDa fragment of actinogelin and alpha-actinins and mapping of their binding sites on the actin molecule by chemical cross-linking.
94 Citations1987Naotoshi Mimura, Atsushi Asano
A conserved actin-binding domain of rat hepatic actinogelin, rat skeletal muscle, and chicken gizzard alpha-actinins was separated into two components having different isoelectric points (peptides A and B) by chromatofocusing and it was shown that peptide A is a precursor of peptide B upon thermolysin digestion.
Cell Motility and the CytoskeletonYeast myosin heavy chain mutant: Maintenance of the cell type specific budding pattern and the normal deposition of chitin and cell wall components requires an intact myosin heavy chain gene
87 Citations1990José R Rodríguez-Medina, Bruce M. Paterson
It is concluded that an intact myosin heavy chain gene is required to maintain the cell type specific budding pattern and the correct localization and deposition of chitin and cell wall components during cell growth and division.
Proceedings of the National Academy of SciencesProteolysis and structure of skeletal muscle actin.
87 Citations1984Dominique Mornet, Kathleen Ue
Under standard conditions, G-actin has been submitted to nine proteases of varying specificity, and in each case the pattern of fragments produced has been studied by NaDodSO4 gel electrophoresis, suggesting that the actin monomer consists of a large region and a small, easily degraded region.
GeneticsDominant suppressors of yeast actin mutations that are reciprocally suppressed.
86 Citations1989A.E. Adams, David Botstein
A gene whose product is likely to interact with yeast actin was identified by the isolation of pseudorevertants carrying dominant suppressors of the temperature-sensitive act1-1 mutation, which indicates mutations in ACT1 and SAC6 can suppress each other's defects.
The Journal of Cell BiologyActin filaments in yeast are unstable in the absence of capping protein or fimbrin.
86 Citations1995Tatiana Karpova, Kelly Tatchell +1 more
It is reported here that capping protein (CP) and fimbrin are both important for actin filament assembly in vivo in Saccharomyces cerevisiae, based on finding decreased actin filaments assembly in CP and fIMbrin mutants and on identifying mutations in actin that enhance the CP phenotype.
Molecular Biology of the CellActin- and tubulin-dependent functions during Saccharomyces cerevisiae mating projection formation.
83 Citations1992Ethan Read, Haruki Okamura +1 more
It is demonstrated that actin is required to restrict cell-surface growth to a defined region for pheromone-induced morphogenesis and suggested that nuclear position and orientation in mating projections depend on direct or indirect interaction of microtubules with actin filaments.
Cell Motility and the CytoskeletonIdentification and molecular characterization of a yeast myosin I
82 Citations1995Holly V. Goodson, James A. Spudich
An unconventional myosin gene (MYO3) in the yeast Saccharomyces cerevisiae is identified and it is shown that it is member of a subclass of unconventionalMyosin proteins originally found only in the amoeboid organisms Dictyostelium and Acanthamoeba.
Molecular Biology of the CellOrganelle-cytoskeletal interactions: actin mutations inhibit meiosis-dependent mitochondrial rearrangement in the budding yeast Saccharomyces cerevisiae.
80 Citations1995Mark Smith, V. R. Simon +2 more
A role for the actin cytoskeleton in the control of mitochondrial position and movements in meiotic yeast is supported, which results in mitochondrial morphology and motility defects at restrictive and permissive temperatures.
Proceedings of the National Academy of SciencesCharge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion.
77 Citations1993M Johara, Yoko Y. Toyoshima +4 more
Measurements indicated that both D24/D25 and E99/E100 are involved in ATP-driven sliding, whereas E360/E361/D363/E364 are not essential for ATP- driven sliding and force generation.
Journal of Molecular BiologyAntibody against the amino terminus of α-actin inhibits actomyosin interactions in the presence of ATP
73 Citations1989Gargi Dasgupta, Emil Reisler
Results, when contrasted with the small effect of Fab on rigor actomyosin binding, suggest ATP-induced changes at the interface of actin and myosin.
The Journal of Cell BiologyActin mutations that show suppression with fimbrin mutations identify a likely fimbrin-binding site on actin.
64 Citations1994Jerry E. Honts, T. Sandrock +3 more
Sequence analysis indicates that all of these mutations change residues that cluster in the small domain of the actin crystal structure, suggesting that this region is an important part of the Sac6p-binding domain.
Molecular Biology of the CellThe rho-GAP encoded by BEM2 regulates cytoskeletal structure in budding yeast.
64 Citations1995Tao Wang, Anthony Bretscher
The identification of seven mutations residing in six genes whose products are required in the absence of Tpm1p provide a genetic link between the GAP encoded by BEM2 and the functional organization of microfilaments and show that bem2 mutations confer benomyl sensitivity and have abnormal microtubule arrays, suggesting that the B EM2 product may also be involved directly or indirectly in regulating microtubules function.
Molecular and Cellular BiologyActin from Saccharomyces cerevisiae.
63 Citations1982Chris L. Greer, Randy Schekman
Journal of Biological ChemistryUnusual metabolism of the yeast actin amino terminus.
63 Citations1991R.K. Cook, David Sheff +1 more
It is concluded that NH2-terminal actin-specific processing is not required for actin function in yeast and three other fungi, yeast are apparently incapable of processing any type of actin precursor, and the stability of a yeast pseudo-class II actin is not affected by the acetylation state of the NH2 terminus.
The Journal of Cell BiologyMapping actin surfaces required for functional interactions in vivo.
62 Citations1994Douglas A. Holtzman, Kenneth F. Wertman +1 more
Genetic interactions between mutant alleles of the yeast actin gene and null allele of the SAC6, ABP1, SLA1, and SLA2 genes demonstrated that the effects of the 21 actin mutations are diverse and allowed four out of seven pseudo-wild-type actin alleles to be distinguished from the wild-type gene for the first time, providing evidence for functional redundancy between different surfaces of actin.
Journal of Cell ScienceIdentification and characterization of a cDNA encoding mouse CAP: a homolog of the yeast adenylyl cyclase associated protein
58 Citations1993Anne B. Vojtek, Jonathan A. Cooper
The isolation of a cDNA encoding a CAP homolog from a higher eukaryote is described and the protein encoded by the mouse CAP cDNA shows extensive homology to the yeast CAP proteins, particularly in the central poly-proline rich region and in the C-terminal domain.
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