GROWTH PATHWAY:

2020 ◽  
pp. 27-50
Keyword(s):  
Growth Pathway

scholarly journals TUP1, CPH1 and EFG1 Make Independent Contributions to Filamentation in Candida albicans

Genetics ◽  
2000 ◽  
Vol 155 (1) ◽  
pp. 57-67 ◽  
Author(s):  
Burkhard R Braun ◽  
Alexander D Johnson
Keyword(s):  
Candida Albicans ◽  
Environmental Conditions ◽  
Target Genes ◽  
Single Cells ◽  
Filamentous Growth ◽  
Surface Proteins ◽  
Pathway Expression ◽  
Separate Pathway ◽  
The Common ◽  
Growth Pathway

Abstract The common fungal pathogen, Candida albicans, can grow either as single cells or as filaments (hyphae), depending on environmental conditions. Several transcriptional regulators have been identified as having key roles in controlling filamentous growth, including the products of the TUP1, CPH1, and EFG1 genes. We show, through a set of single, double, and triple mutants, that these genes act in an additive fashion to control filamentous growth, suggesting that each gene represents a separate pathway of control. We also show that environmentally induced filamentous growth can occur even in the absence of all three of these genes, providing evidence for a fourth regulatory pathway. Expression of a collection of structural genes associated with filamentous growth, including HYR1, ECE1, HWP1, ALS1, and CHS2, was monitored in strains lacking each combination of TUP1, EFG1, and CPH1. Different patterns of expression were observed among these target genes, supporting the hypothesis that these three regulatory proteins engage in a network of individual connections to downstream genes and arguing against a model whereby the target genes are regulated through a central filamentous growth pathway. The results suggest the existence of several distinct types of filamentous forms of C. albicans, each dependent on a particular set of environmental conditions and each expressing a unique set of surface proteins.

MTA3, a Mi-2/NuRD complex subunit, regulates an invasive growth pathway in breast cancer

2004 ◽  
Vol 4 (1) ◽  
pp. 13-15
Author(s):  
Sylvia Julien-Grille ◽  
Alfonso Bellacosa ◽  
Lionel Larue
Keyword(s):  
Breast Cancer ◽  
Invasive Growth ◽  
Nurd Complex ◽  
Growth Pathway

Chemical communication between regenerating motor axons and Schwann cells in the growth pathway

2009 ◽  
Vol 30 (3) ◽  
pp. 366-375 ◽  
Author(s):  
Gerta Vrbova ◽  
Neeraj Mehra ◽  
Harei Shanmuganathan ◽  
Neil Tyreman ◽  
Melitta Schachner ◽  
...  
Keyword(s):  
Schwann Cells ◽  
Chemical Communication ◽  
Motor Axons ◽  
Growth Pathway

scholarly journals Ragulator and SLC38A9 activate the Rag GTPases through noncanonical GEF mechanisms

2018 ◽  
Vol 115 (38) ◽  
pp. 9545-9550 ◽  
Author(s):  
Kuang Shen ◽  
David M. Sabatini
Keyword(s):  
Subcellular Localization ◽  
Transmembrane Protein ◽  
Mechanistic Target Of Rapamycin ◽  
Rag Gtpases ◽  
Locking Mechanism ◽  
Mtorc1 Pathway ◽  
Loaded State ◽  
Rag Gtpase ◽  
And Control ◽  
Growth Pathway

The mechanistic target of rapamycin complex 1 (mTORC1) growth pathway detects nutrients through a variety of sensors and regulators that converge on the Rag GTPases, which form heterodimers consisting of RagA or RagB tightly bound to RagC or RagD and control the subcellular localization of mTORC1. The Rag heterodimer uses a unique “locking” mechanism to stabilize its active (GTPRagA–RagCGDP) or inactive (GDPRagA–RagCGTP) nucleotide states. The Ragulator complex tethers the Rag heterodimer to the lysosomal surface, and the SLC38A9 transmembrane protein is a lysosomal arginine sensor that upon activation stimulates mTORC1 activity through the Rag GTPases. How Ragulator and SLC38A9 control the nucleotide loading state of the Rag GTPases remains incompletely understood. Here we find that Ragulator and SLC38A9 are each unique guanine exchange factors (GEFs) that collectively push the Rag GTPases toward the active state. Ragulator triggers GTP release from RagC, thus resolving the locked inactivated state of the Rag GTPases. Upon arginine binding, SLC38A9 converts RagA from the GDP- to the GTP-loaded state, and therefore activates the Rag GTPase heterodimer. Altogether, Ragulator and SLC38A9 act on the Rag GTPases to activate the mTORC1 pathway in response to nutrient sufficiency.

Abstract 481: Distinct and overlapping patterns of B-cell growth pathway mutations in CD5-negative B-cell lymphoproliferative disorders

2019 ◽  
Author(s):  
Sophia Shaddy ◽  
Weiqiang Zhao ◽  
Huolin Tu ◽  
Brianna Sisson ◽  
Rongqin Ren ◽  
...  
Keyword(s):  
Cell Growth ◽  
B Cell ◽  
Lymphoproliferative Disorders ◽  
Growth Pathway

Growth Pathway of Pt Clusters on α-Al2O3(0001) Surface

2007 ◽  
Vol 111 (37) ◽  
pp. 13786-13793 ◽  
Author(s):  
Chenggang Zhou ◽  
Jinping Wu ◽  
T. J. Dhilip Kumar ◽  
Naduvalath Balakrishnan ◽  
Robert C. Forrey ◽  
...  
Keyword(s):  
Α Al2o3 ◽  
Growth Pathway

scholarly journals Cdc42p-Interacting Protein Bem4p Regulates the Filamentous-Growth Mitogen-Activated Protein Kinase Pathway

2014 ◽  
Vol 35 (2) ◽  
pp. 417-436 ◽  
Author(s):  
Andrew Pitoniak ◽  
Colin A. Chavel ◽  
Jacky Chow ◽  
Jeremy Smith ◽  
Diawoye Camara ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Mapk Pathway ◽  
Filamentous Growth ◽  
Cell Polarization ◽  
Mitogen Activated Protein Kinase ◽  
Specific Response ◽  
Ph Domain ◽  
Interacting Protein ◽  
Mitogen Activated Protein ◽  
Growth Pathway

The ubiquitous Rho (Ras homology) GTPase Cdc42p can function in different settings to regulate cell polarity and cellular signaling. How Cdc42p and other proteins are directed to function in a particular context remains unclear. We show that the Cdc42p-interacting protein Bem4p regulates the mitogen-activated protein kinase (MAPK) pathway that controls filamentous growth inSaccharomyces cerevisiae. Bem4p controlled the filamentous-growth pathway but not other MAPK pathways (mating or high-osmolarity glycerol response [HOG]) that also require Cdc42p and other shared components. Bem4p associated with the plasma membrane (PM) protein, Sho1p, to regulate MAPK activity and cell polarization under nutrient-limiting conditions that favor filamentous growth. Bem4p also interacted with the major activator of Cdc42p, the guanine nucleotide exchange factor (GEF) Cdc24p, which we show also regulates the filamentous-growth pathway. Bem4p interacted with the pleckstrin homology (PH) domain of Cdc24p, which functions in an autoinhibitory capacity, and was required, along with other pathway regulators, to maintain Cdc24p at polarized sites during filamentous growth. Bem4p also interacted with the MAPK kinase kinase (MAPKKK) Ste11p. Thus, Bem4p is a new regulator of the filamentous-growth MAPK pathway and binds to general proteins, like Cdc42p and Ste11p, to promote a pathway-specific response.

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