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Hallett, Mark A.; Lo, H. Shuen; Bender, Alan

doi:10.1186/1471-2121-3-16

Cited by 33 publications

(18 citation statements)

References 30 publications

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“…The PH domains of Boi1/2p interact with Sec1p PH Boi1 and PH Boi2 bind to lipids and active Cdc42p (Bender et al, 1996;Hallett et al, 2002). Neither of these activities is specifically linked to the accumulation of post-Golgi vesicles.…”

Section: Depletion Of Boi1/2p Disrupts the Fusion Of Secretory Vesiclmentioning

confidence: 99%

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The cell polarity proteins Boi1p and Boi2p stimulate vesicle fusion at the plasma membrane of yeast cells

Kustermann

Rieger

et al. 2017

Journal of Cell Science

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Eukaryotic cells can direct secretion to defined regions of their plasma membrane. These regions are distinguished by an elaborate architecture of proteins and lipids that are specialized to capture and fuse post-Golgi vesicles. Here, we show that the proteins Boi1p and Boi2p are important elements of this area of active exocytosis at the tip of growing yeast cells. Cells lacking Boi1p and Boi2p accumulate secretory vesicles in their buds. The essential PH domains of Boi1p and Boi2p interact with Sec1p, a protein required for SNARE complex formation and vesicle fusion. Sec1p loses its tip localization in cells depleted of Boi1p and Boi2p but overexpression of Sec1p can partially compensate for their loss. The capacity to simultaneously bind phospholipids, Sec1p, multiple subunits of the exocyst, Cdc42p and the module for generating active Cdc42p identify Boi1p and Boi2p as essential mediators between exocytosis and polar growth.

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Section: Depletion Of Boi1/2p Disrupts the Fusion Of Secretory Vesiclmentioning

confidence: 99%

“…4E; Fig. S2A) (Hallett et al, 2002). To find out whether binding to Cdc42 is equally important, we first searched for residues in PH Boi1 that are required for complex formation with active Cdc42p.…”

Section: Binding To Cdc42p Is Not Essential For the Role Of Boi1/2p Imentioning

confidence: 99%

The cell polarity proteins Boi1p and Boi2p stimulate vesicle fusion at the plasma membrane of yeast cells

Kustermann

Rieger

et al. 2017

Journal of Cell Science

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“…Whether the PH domain of Cdc24 binds phosphoinositides is unknown. However, the PH domain of Boi1 does bind PI4,5P2 (31). Furthermore, Boi1 PH domain point mutants impaired in PI4,5P2 binding fail to function or localize to the bud cortex (31).…”

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confidence: 99%

“…However, the PH domain of Boi1 does bind PI4,5P2 (31). Furthermore, Boi1 PH domain point mutants impaired in PI4,5P2 binding fail to function or localize to the bud cortex (31). The Cdc42 scaffold protein Bem1 possesses a phox homology domain that binds phosphatidylinositol 3-phosphate (PI3P (32)), which has a prominent role in protein trafficking to the vacuole (24).…”

mentioning

confidence: 99%

The p21-activated Protein Kinase-related Kinase Cla4 Is a Coincidence Detector of Signaling by Cdc42 and Phosphatidylinositol 4-Phosphate

Wild

Lemmon

et al. 2004

Journal of Biological Chemistry

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Signal transduction pathways that co-regulate a given biological process often are organized into networks by molecules that act as coincidence detectors. Phosphoinositides and the Rho-type GTPase Cdc42 regulate overlapping processes in all eukaryotic cells. However, the coincidence detectors that link these pathways into networks remain unknown. Here we show that the p21-activated protein kinase-related kinase Cla4 of yeast integrates signaling by Cdc42 and phosphatidylinositol 4-phosphate (PI4P). We found that the Cla4 pleckstrin homology (PH) domain binds in vitro to several phosphoinositide species. To determine which phosphoinositides regulate Cla4 in vivo, we analyzed phosphatidylinositol kinase mutants (stt4, mss4, and pik1). This indicated that the plasma membrane pool of PI4P, but not phosphatidylinositol 4,5-bisphosphate or the Golgi pool of PI4P, is required for localization of Cla4 to sites of polarized growth. A combination of the Cdc42-binding and PH domains of Cla4 was necessary and sufficient for localization to sites of polarized growth. Point mutations affecting either domain impaired the ability of Cla4 to regulate cell morphogenesis and the mitotic exit network (localization of Lte1). Therefore, Cla4 must retain the ability to bind both Cdc42 and phosphoinositides, the hallmark of a coincidence detector. PI4P may recruit Cla4 to the plasma membrane where Cdc42 activates its kinase activity and refines its localization to cortical sites of polarized growth. In mammalian cells, the myotonic dystrophy-related Cdc42-binding kinase possesses p21-binding and PH domains, suggesting that this kinase may be a coincidence detector of signaling by Cdc42 and phosphoinositides.

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“…Among these DFFMs we noticed that Tpk1-mediated phosphorylation of the Boi1-Opi1 and the Boi1-Osh3 protein pairs from the SCPnet were required for growth in the presence of 7 and 6 chemicals, respectively. Of these, Boi1 binds acidic phospholipids via its PH domain and is required by the “NoCut” checkpoint pathway, which delays the completion of cytokinesis in response to anaphase defects 81, 82 . On the other hand Opi1 is a transcriptional repressor of phospholipid biosynthetic genes 83 and is also activated by Tpk1-catalyzed phosphorylation 84 .…”

Section: Resultsmentioning

confidence: 99%

Robustness and evolvability in natural chemical resistance: identification of novel systems properties, biochemical mechanisms and regulatory interactions

et al. 2010

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A vast amount of data on the natural resistance of Saccharomyces cerevisiae to a diverse array of chemicals has been generated over the past decade (chemical genetics). We endeavored to use this data to better characterize the “systems” level properties of this phenomenon. By collating data from over 30 different genome-scale studies on growth of gene deletion mutants in presence of diverse chemicals, we assembled the largest currently available gene-chemical network. We also derived a second gene-gene network that links genes with significantly overlapping chemical-genetic profiles. We analyzed properties of these networks and investigated their significance by overlaying various sources of information, such as presence of TATA boxes in their promoters (which typically correlate with transcriptional noise), association with TFIID or SAGA, and propensity to function as phenotypic capacitors. We further combined these networks with ubiquitin and protein kinase-substrate networks to understand chemical tolerance in the context of major post-translational regulatory processes. Hubs in the gene-chemical network (multidrug resistance genes) are notably enriched for phenotypic capacitors (buffers against phenotypic variation), suggesting the generality of these players in buffering mechanistically unrelated deleterious forces impinging on the cell. More strikingly, analysis of the gene-gene network derived from the gene-chemical network uncovered another set of genes that appear to function in providing chemical tolerance in a cooperative manner. These appear to be enriched in lineage-specific and rapidly diverging members that also show a corresponding tendency for SAGA-dependent regulation, evolutionary divergence and noisy expression patterns. This set represents a previously underappreciated component of the chemical response that enables cells to explore alternative survival strategies. Thus, systems robustness and evolvability are simultaneously active as general forces in tolerating environmental variation. We also recover the actual genes involved in the above-discussed network properties and predict the biochemistry of their products. Certain key components of the ubiquitin system (e.g. Rcy1, Wss1 and Ubp16), peroxisome recycling (e.g. Irs4) and phosphorylation cascades (e.g. NPR1, MCK1 and HOG) are major participants and regulators of chemical resistance. We also show that a major subnetwork boosting mitochondrial protein synthesis is important for exploration of alternative survival strategies under chemical stress. Further, we find evidence that cellular exploration of survival strategies under chemical stress and secondary metabolism draw from a common pool of biochemical players (e.g. acetyltransferases and a novel NTN hydrolase).

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Untitled

Cited by 33 publications

References 30 publications

The cell polarity proteins Boi1p and Boi2p stimulate vesicle fusion at the plasma membrane of yeast cells

The cell polarity proteins Boi1p and Boi2p stimulate vesicle fusion at the plasma membrane of yeast cells

The p21-activated Protein Kinase-related Kinase Cla4 Is a Coincidence Detector of Signaling by Cdc42 and Phosphatidylinositol 4-Phosphate

Robustness and evolvability in natural chemical resistance: identification of novel systems properties, biochemical mechanisms and regulatory interactions

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