PMID- 9315645
OWN - NLM
STAT- MEDLINE
DCOM- 19971023
LR  - 20211203
IS  - 0270-7306 (Print)
IS  - 1098-5549 (Electronic)
IS  - 0270-7306 (Linking)
VI  - 17
IP  - 10
DP  - 1997 Oct
TI  - Multiple regulatory domains on the Byr2 protein kinase.
PG  - 5876-87
AB  - Byr2 protein kinase, a homolog of mammalian mitogen-activated protein 
      kinase/extracellular signal-regulated kinase kinase (MEKK) and Saccharomyces 
      cerevisiae STE11, is required for pheromone-induced sexual differentiation in the 
      fission yeast Schizosaccharomyces pombe. Byr2 functions downstream of Ste4, Ras1, 
      and the membrane-associated receptor-coupled heterotrimeric G-protein alpha 
      subunit, Gpa1. Byr2 has a distinctive N-terminal kinase regulatory domain and a 
      characteristic C-terminal kinase catalytic domain. Ste4 and Ras1 interact with 
      the regulatory domain of Byr2 directly. Here, we define the domains of Byr2 that 
      bind Ste4 and Ras1 and show that the Byr2 regulatory domain binds to the 
      catalytic domain in the two-hybrid system. Using Byr2 mutants, we demonstrate 
      that these direct physical interactions are all required for proper signaling. In 
      particular, the physical association between Byr2 regulatory and catalytic 
      domains appears to result in autoinhibition, the loss of which results in kinase 
      activation. Furthermore, we provide evidence that Shk1, the S. pombe homolog of 
      the STE20 protein kinase, can directly antagonize the Byr2 intramolecular 
      interaction, possibly by phosphorylating Byr2.
FAU - Tu, H
AU  - Tu H
AD  - Cold Spring Harbor Laboratory, New York 11724, USA.
FAU - Barr, M
AU  - Barr M
FAU - Dong, D L
AU  - Dong DL
FAU - Wigler, M
AU  - Wigler M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (Fungal Proteins)
RN  - 0 (GTP-Binding Protein beta Subunits)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Schizosaccharomyces pombe Proteins)
RN  - 0 (Ste4 protein, S cerevisiae)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (p21-Activated Kinases)
RN  - EC 2.7.11.1 (shk1 protein, S pombe)
RN  - EC 2.7.11.25 (BYR2 protein, S pombe)
RN  - EC 2.7.11.25 (MAP Kinase Kinase Kinases)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 3.6.5.1 (Heterotrimeric GTP-Binding Proteins)
RN  - EC 3.6.5.2 (RAS1 protein, S cerevisiae)
RN  - EC 3.6.5.2 (Ras1 protein, S pombe)
RN  - EC 3.6.5.2 (ras Proteins)
SB  - IM
MH  - Cloning, Molecular
MH  - Fungal Proteins/genetics/*metabolism
MH  - *GTP-Binding Protein beta Subunits
MH  - GTP-Binding Proteins/metabolism
MH  - Genes, Fungal/genetics
MH  - *Heterotrimeric GTP-Binding Proteins
MH  - *MAP Kinase Kinase Kinases
MH  - Point Mutation
MH  - Protein Binding
MH  - Protein Kinases/genetics/*metabolism
MH  - Protein Serine-Threonine Kinases/metabolism
MH  - Recombinant Fusion Proteins
MH  - Saccharomyces cerevisiae/genetics
MH  - *Saccharomyces cerevisiae Proteins
MH  - Schizosaccharomyces/*enzymology/genetics/physiology
MH  - *Schizosaccharomyces pombe Proteins
MH  - Spores, Fungal
MH  - p21-Activated Kinases
MH  - ras Proteins/metabolism
PMC - PMC232435
EDAT- 1997/10/07 00:00
MHDA- 1997/10/07 00:01
PMCR- 1997/10/01
CRDT- 1997/10/07 00:00
PHST- 1997/10/07 00:00 [pubmed]
PHST- 1997/10/07 00:01 [medline]
PHST- 1997/10/07 00:00 [entrez]
PHST- 1997/10/01 00:00 [pmc-release]
AID - 10.1128/MCB.17.10.5876 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1997 Oct;17(10):5876-87. doi: 10.1128/MCB.17.10.5876.