Development of cell polarity in budding yeast

Govindan, Brinda; Novick, Peter

doi:10.1002/jez.1402730505

Cited by 18 publications

(10 citation statements)

References 222 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Myo2p may serve as an actin-based motor that translocates secretory vesicles to growth sites ( Figure 6). However, despite extensive effort, no direct evidence for this model exists (114). An alternative model is that Myo2p helps localize and organize actin at growth sites, perhaps serving as a cortical tether for actin filaments.…”

Section: The Role Of the Cytoskeletonmentioning

confidence: 94%

“…ACTIN Actin is essential for polarized cell growth in yeast and is present in two forms. Actin patches localize at the cortex, primarily in the bud, and actin cables run longitudinally along the length of the cell and often intersect actin patches at their ends (3,114,150,220). Electron microscopic studies indicate that the cortical actin patches are sites of plasma membrane invaginations (220).…”

Section: The Role Of the Cytoskeletonmentioning

confidence: 97%

See 1 more Smart Citation

Cell Polarity and Morphogenesis in Budding Yeast

Madden

Snyder

1998

Annu. Rev. Microbiol.

250

231

View full text Add to dashboard Cite

Eukaryotic cells respond to intracellular and extracellular cues to direct asymmetric cell growth and division. The yeast Saccharomyces cerevisiae undergoes polarized growth at several times during budding and mating and is a useful model organism for studying asymmetric growth and division. In recent years, many regulatory and cytoskeletal components important for directing and executing growth have been identified, and molecular mechanisms have been elucidated in yeast. Key signaling pathways that regulate polarization during the cell cycle and mating response have been described. Since many of the components important for polarized cell growth are conserved in other organisms, the basic mechanisms mediating polarized cell growth are likely to be universal among eukaryotes.

show abstract

Section: The Role Of the Cytoskeletonmentioning

confidence: 94%

Section: The Role Of the Cytoskeletonmentioning

confidence: 97%

Cell Polarity and Morphogenesis in Budding Yeast

Madden

Snyder

1998

Annu. Rev. Microbiol.

250

231

View full text Add to dashboard Cite

show abstract

“…Such activating factors could serve to spatially restrict Sso1p-Sec9p activity to the bud tip, the site of exocytosis in yeast 35 . In principal, any specialized feature of the bud tip could serve to release Sso1NT inhibition.…”

Section: Functional Implicationsmentioning

confidence: 99%

Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p

Nicholson

Munson

Miller

et al. 1998

Nat Struct Mol Biol

211

257

View full text Add to dashboard Cite

The fusion of intracellular transport vesicles with their target membranes requires the assembly of SNARE proteins anchored in the apposed membranes. Here we use recombinant cytoplasmic domains of the yeast SNAREs involved in Golgi to plasma membrane trafficking to examine this assembly process in vitro. Binary complexes form between the target membrane SNAREs Sso1p and Sec9p; these binary complexes can subsequently bind to the vesicle SNARE Snc2p to form ternary complexes. Binary and ternary complex assembly are accompanied by large increases in alpha-helical structure, indicating that folding and complex formation are linked. Surprisingly, we find that binary complex formation is extremely slow, with a second-order rate constant of approximately 3 M(-1) s(-1). An N-terminal regulatory domain of Sso1p accounts for slow assembly, since in its absence complexes assemble 2,000-fold more rapidly. Once binary complexes form, ternary complex formation is rapid and is not affected by the presence of the regulatory domain. Our results imply that proteins that accelerate SNARE assembly in vivo act by relieving inhibition by this regulatory domain.

show abstract

“…For this purpose, vesicles loaded with components required for the cell wall expansion are transported to active sites of growth over a network of polarized microtubes [27]. Therefore, polarized growth requires proteins involved in cytoskeleton functions and secretory endocytic machinery [28]. The plasma membrane consists of different sub-domains defined by its distribution of sphingolipids and sterols.…”

Section: Introductionmentioning

confidence: 99%

Functional Characterization of Aspergillus nidulans ypkA, a Homologue of the Mammalian Kinase SGK

et al. 2013

View full text Add to dashboard Cite

The serum- and glucocorticoid-regulated protein kinase (SGK) is an AGC kinase involved in signal cascades regulated by glucocorticoid hormones and serum in mammals. The Saccharomyces cerevisiae ypk1 and ypk2 genes were identified as SGK homologues and Ypk1 was shown to regulate the balance of sphingolipids between the inner and outer plasma membrane. This investigation characterized the Aspergillus nidulans YPK1 homologue, YpkA, representing the first filamentous fungal YPK1 homologue. Two conditional mutant strains were constructed by replacing the endogenous ypk1 promoter with two different regulatable promoters, alcA (from the alcohol dehydrogenase gene) and niiA (from the nitrate reductase gene). Both constructs confirmed that ypkA was an essential gene in A. nidulans. Repression of ypkA caused decreased radial growth, a delay in conidial germination, deficient polar axis establishment, intense branching during late stages of growth, a lack of asexual spores, and a terminal phenotype. Membrane lipid polarization, endocytosis, eisosomes and vacuolar distribution were also affected by ypkA repression, suggesting that YpkA plays a role in hyphal morphogenesis via coordinating the delivery of cell membrane and wall constituents to the hyphal apex. The A. nidulans Pkh1 homologue pkhA was also shown to be an essential gene, and preliminary genetic analysis suggested that the ypkA gene is not directly downstream of pkhA or epistatic to pkhA, rather, ypkA and pkhA are genetically independent or in parallel. BarA is a homologue of the yeast Lag1 acyl-CoA-dependent ceramide synthase, which catalyzes the condensation of phytosphingosine with a fatty acyl-CoA to form phytoceramide. When barA was absent, ypkA repression was lethal to the cell. Therefore, there appears to be a genetic interaction between ypkA, barA, and the sphingolipid synthesis. Transcriptional profiling of ypkA overexpression and down-regulation revealed several putative YpkA targets associated with the observed phenotypes.

show abstract

Development of cell polarity in budding yeast

Cited by 18 publications

References 222 publications

Cell Polarity and Morphogenesis in Budding Yeast

Cell Polarity and Morphogenesis in Budding Yeast

Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p

Functional Characterization of Aspergillus nidulans ypkA, a Homologue of the Mammalian Kinase SGK

Contact Info

Product

Resources

About