PMID- 10330148
OWN - NLM
STAT- MEDLINE
DCOM- 19990617
LR  - 20210526
IS  - 0270-7306 (Print)
IS  - 1098-5549 (Electronic)
IS  - 0270-7306 (Linking)
VI  - 19
IP  - 6
DP  - 1999 Jun
TI  - Separation and characterization of the activated pool of colony-stimulating 
      factor 1 receptor forming distinct multimeric complexes with signalling molecules 
      in macrophages.
PG  - 4079-92
AB  - Colony-stimulating factor 1 (CSF-1) triggers the activation of intracellular 
      proteins in macrophages through selective assembly of signalling complexes. The 
      separation of multimeric complexes of the CSF-1 receptor (CSF-1R) by 
      anion-exchange chromatography enabled the enrichment of low-stoichiometry 
      complexes. A significant proportion of the receptor in CSF-1-stimulated cells 
      that neither possessed detectable tyrosine kinase activity nor formed complexes 
      was separated from the receptor pool displaying autokinase activity that formed 
      chromatographically distinct multimeric complexes. A small pool of CSF-1R formed 
      a multimeric complex with phosphatidylinositol-3 kinase (PI-3 kinase), SHP-1, 
      Grb2, Shc, c-Src, Cbl, and a significant number of tyrosine-phosphorylated 
      proteins in CSF-1-stimulated cells. The complex showed a considerable amount of 
      CSF-1R complex-associated kinase activity. A detectable level of the complex was 
      also present in untreated cells. PI-3 kinase in the multimeric complex displayed 
      low lipid kinase activity despite the association with several proteins. The 
      major pool of activated CSF-1R formed transient multimeric complexes with 
      distinctly different tyrosine-phosphorylated proteins, which included STAT3 but 
      also PI-3 kinase, Shc, SHP-1, and Grb2. A significant level of lipid kinase 
      activity was detected in PI-3 kinase in the latter complexes. The different 
      specific enzyme activities of PI-3 kinase in these complexes support the notion 
      that the activity of PI-3 kinase is modulated by its association with CSF-1R and 
      other associated cellular proteins. Specific structural proteins associated with 
      the separate CSF-1R multimeric complexes upon CSF-1 stimulation and the presence 
      of the distinct pools of the CSF-1R were dependent on the integrity of the 
      microtubular network.
FAU - Kanagasundaram, V
AU  - Kanagasundaram V
AD  - Department of Medicine, University of Melbourne, Royal Melbourne Hospital, 
      Parkville, Victoria 3050, Australia. v.kanagasundaram@medicine.unimelb.edu.au
FAU - Jaworowski, A
AU  - Jaworowski A
FAU - Byrne, R
AU  - Byrne R
FAU - Hamilton, J A
AU  - Hamilton JA
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (Indoleacetic Acids)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Receptors, Colony-Stimulating Factor)
RN  - 22144-77-0 (Cytochalasin D)
RN  - 42HK56048U (Tyrosine)
RN  - 6U1S09C61L (indoleacetic acid)
RN  - EC 2.7.- (Phosphotransferases)
RN  - EC 2.7.1.- (Phosphatidylinositol 3-Kinases)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 11)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 6)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
RN  - EC 3.1.3.48 (Ptpn11 protein, mouse)
RN  - EC 3.1.3.48 (Ptpn6 protein, mouse)
RN  - SH1WY3R615 (Nocodazole)
SB  - IM
MH  - Animals
MH  - Cell Line
MH  - Chromatography, Ion Exchange
MH  - Cytochalasin D/pharmacology
MH  - Indoleacetic Acids/pharmacology
MH  - Intracellular Signaling Peptides and Proteins
MH  - Macrophages/*metabolism
MH  - Mice
MH  - Models, Biological
MH  - Nocodazole/pharmacology
MH  - Phosphatidylinositol 3-Kinases/chemistry
MH  - Phosphorylation
MH  - Phosphotransferases/metabolism
MH  - Precipitin Tests
MH  - Protein Conformation
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 11
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 6
MH  - Protein Tyrosine Phosphatases/chemistry
MH  - Receptors, Colony-Stimulating Factor/*chemistry
MH  - *Signal Transduction
MH  - Subcellular Fractions
MH  - Time Factors
MH  - Tyrosine/metabolism
PMC - PMC104367
EDAT- 1999/05/18 00:00
MHDA- 1999/05/18 00:01
CRDT- 1999/05/18 00:00
PHST- 1999/05/18 00:00 [pubmed]
PHST- 1999/05/18 00:01 [medline]
PHST- 1999/05/18 00:00 [entrez]
AID - 1255 [pii]
AID - 10.1128/MCB.19.6.4079 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1999 Jun;19(6):4079-92. doi: 10.1128/MCB.19.6.4079.