ŠPÍREK, Mário, Zhengchang LIU, Janet THORNTON and Ronald BUTOW. Activation of the SPS Amino Acid-Sensing Pathway in Saccharomyces cerevisiae Correlates with the Phosphorylation State of a Sensor Component, Ptr3. Molecular and Cellular Biology. Washington, D.C.: ASM, vol. 28, No 2, p. 551–563. ISSN 0270-7306. 2008.
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Basic information
Original name Activation of the SPS Amino Acid-Sensing Pathway in Saccharomyces cerevisiae Correlates with the Phosphorylation State of a Sensor Component, Ptr3
Name in Czech Aktivace SPS aminokyseliny detekující dráhy v Saccharomyces cerevisae koreluje s fosforylačním stavem senzorového komponentu Ptr3
Authors ŠPÍREK, Mário (703 Slovakia, guarantor), Zhengchang LIU (156 China), Janet THORNTON (840 United States of America) and Ronald BUTOW (840 United States of America).
Edition Molecular and Cellular Biology, Washington, D.C. ASM, 2008, 0270-7306.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 5.942
RIV identification code RIV/00216224:14310/08:00035918
Organization unit Faculty of Science
UT WoS 000252283300003
Keywords (in Czech) SPS aminokyseliny detekující dráha; ptr3, fosforylace; kvasinka
Keywords in English SPS amino-acid sensing pathway; Ptr3; phosphorylation; yeast
Tags phosphorylation, Ptr3, SPS amino-acid sensing pathway, Yeast
Tags International impact, Reviewed
Changed by Changed by: RNDr. Mário Špírek, PhD., učo 107122. Changed: 23/6/2009 14:18.
Abstract
Cells of the budding yeast Saccharomyces cerevisiae sense extracellular amino acids and activate expression of amino acid permeases through the SPS-sensing pathway, which consists of Ssy1, an amino acid sensor on the plasma membrane, and two downstream factors, Ptr3 and Ssy5. Upon activation of SPS signaling, two transcription factors, Stp1 and Stp2, undergo Ssy5-dependent proteolytic processing that enables their nuclear translocation. Here we show that Ptr3 is a phosphoprotein whose hyperphosphorylation is increased by external amino acids and is dependent on Ssy1 but not on Ssy5. A deletion mutation in GRR1, encoding a component of the SCFGrr1 E3 ubiquitin ligase, blocks amino acid-induced hyperphosphorylation of Ptr3. We found that two casein kinase I (CKI) proteins, Yck1 and Yck2, previously identified as positive regulators of SPS signaling, are required for hyperphosphorylation of Ptr3. Loss- and gain-of-function mutations in PTR3 result in decreased and increased Ptr3 hyperphosporylation, respectively. We found that a defect in PP2A phosphatase activity leads to the hyperphosphorylation of Ptr3 and constitutive activation of SPS signaling. Two-hybrid analysis revealed interactions between the N-terminal signal transduction domain of Ssy1 with Ptr3 and Yck1. Our findings reveal that CKI and PP2A phosphatase play antagonistic roles in SPS sensing by regulating Ptr3 phosphorylation.
Abstract (in Czech)
Ptr3 je fosfoprotein, kterého hyperfosforylace je zvýšená externími aminokyselinami a je závislá na Ssy1, ale ne na Ssy5. Deleční mutance Grr1 genu, kódujícího komponent SCFGrr1 E3 ubikvitin ligázy, blokuje aminokyselinami indukovanou hyperfosforylaci Ptr3 proteinu. Dvé kazein kinázy I (CKI) proteiny, Yck1 a Yck2, předtím identifikované jako pozitivní regulátory SPS signalizaci, jsou zapotřebí pro hyperfosforylaci Ptr3 proteinu.
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