Activation of the SPS Amino Acid-Sensing Pathway in
Saccharomyces cerevisiae Correlates with the Phosphorylation
State of a Sensor Component, Ptr3

J 2008

Activation of the SPS Amino Acid-Sensing Pathway in Saccharomyces cerevisiae Correlates with the Phosphorylation State of a Sensor Component, Ptr3

ŠPÍREK, Mário, Zhengchang LIU, Janet THORNTON and Ronald BUTOW

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

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

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

Abstract

ORIG CZ

V originále

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.

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.

Citovat

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, 2008, vol. 28, No 2, p. 551–563. ISSN 0270-7306.

@article{838003,
   author = {Špírek, Mário and Liu, Zhengchang and Thornton, Janet and Butow, Ronald},
   article_location = {Washington, D.C.},
   article_number = {2},
   keywords = {SPS amino-acid sensing pathway; Ptr3; phosphorylation; yeast},
   language = {eng},
   issn = {0270-7306},
   journal = {Molecular and Cellular Biology},
   title = {Activation of the SPS Amino Acid-Sensing Pathway in Saccharomyces cerevisiae Correlates with the Phosphorylation State of a Sensor Component, Ptr3},
   url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=17984223},
   volume = {28},
   year = {2008}
}

TY  - JOUR
ID  - 838003
AU  - Špírek, Mário - Liu, Zhengchang - Thornton, Janet - Butow, Ronald
PY  - 2008
TI  - Activation of the SPS Amino Acid-Sensing Pathway in Saccharomyces cerevisiae Correlates with the Phosphorylation State of a Sensor Component, Ptr3
JF  - Molecular and Cellular Biology
VL  - 28
IS  - 2
SP  - 551–563
EP  - 551–563
PB  - ASM
SN  - 02707306
KW  - SPS amino-acid sensing pathway
KW  - Ptr3
KW  - phosphorylation
KW  - yeast
UR  - http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=17984223
N2  - 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.
ER  -

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. \textit{Molecular and Cellular Biology}. Washington, D.C.: ASM, 2008, vol.~28, No~2, p.~551–563. ISSN~0270-7306.

Detailed Information on Publication Record