PMID- 10644978
OWN - NLM
STAT- MEDLINE
DCOM- 20000207
LR  - 20181130
IS  - 0950-9232 (Print)
IS  - 0950-9232 (Linking)
VI  - 19
IP  - 1
DP  - 2000 Jan 6
TI  - PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated mitogenesis.
PG  - 39-50
AB  - PSM/SH2-B has been described as a cellular partner of the FcepsilonRI receptor,
      insulin receptor (IR), insulin-like growth factor-I (IGF-I) receptor (IGF-IR),
      and nerve growth factor receptor (TrkA). A function has been proposed in neuronal
      differentiation and development but its role in other signaling pathways is still
      unclear. To further elucidate the physiologic role of PSM we have identified
      additional mitogenic receptor tyrosine kinases as putative PSM partners including
      platelet-derived growth factor (PDGF) receptor (PDGFR) beta, hepatocyte growth
      factor receptor (Met), and fibroblast growth factor receptor. We have mapped Y740
      as a site of PDGFR beta that is involved in the association with PSM. We have
      further investigated the putative role of PSM in mitogenesis with three
      independent experimental strategies and found that all consistently suggested a
      role as a positive, stimulatory signaling adapter in normal NIH3T3 and baby
      hamster kidney fibroblasts. (1) PSM expression from cDNA using an
      ecdysone-regulated transient expression system stimulated PDGF-BB-, IGF-I-, and
      insulin- but not EGF-induced DNA synthesis in an ecdysone dose-responsive
      fashion; (2) Microinjection of the (dominant negative) PSM SH2 domain interfered 
      with PDGF-BB- and insulin-induced DNA synthesis; and (3) A peptide mimetic of the
      PSM Pro-rich putative SH3 domain-binding region interfered with PDGF-BB-, IGF-I-,
      and insulin- but not with EGF-induced DNA synthesis in NIH3T3 fibroblasts. This
      experiment was based on cell-permeable fusion peptides with the Drosophila
      antennapedia homeodomain which effectively traverse the plasma membrane of
      cultured cells. These experimental strategies independently suggest that PSM
      functions as a positive, stimulatory, mitogenic signaling mediator in PDGF-BB,
      IGF-I, and insulin but not in EGF action. This function appears to involve the
      PSM SH2 domain as well as the Pro-rich putative SH3 domain binding region. Our
      findings support the model that PSM participates as an adapter in various
      mitogenic signaling mechanisms by linking an activated (receptor)
      phospho-tyrosine to the SH3 domain of an unknown cellular partner.
FAU - Riedel, H
AU  - Riedel H
AD  - Department of Biological Sciences, Wayne State University, Detroit, Michigan, MI 
      48202, USA.
FAU - Yousaf, N
AU  - Yousaf N
FAU - Zhao, Y
AU  - Zhao Y
FAU - Dai, H
AU  - Dai H
FAU - Deng, Y
AU  - Deng Y
FAU - Wang, J
AU  - Wang J
LA  - eng
GR  - R01 CA77873/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Oncogene
JT  - Oncogene
JID - 8711562
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Carrier Proteins)
RN  - 0 (Insulin)
RN  - 0 (Platelet-Derived Growth Factor)
RN  - 0 (Proto-Oncogene Proteins c-sis)
RN  - 0 (Sh2bpsm1 protein, mouse)
RN  - 1B56C968OA (Becaplermin)
RN  - 3604-87-3 (Ecdysone)
RN  - 67763-96-6 (Insulin-Like Growth Factor I)
RN  - 9007-49-2 (DNA)
RN  - EC 2.7.1.- (Phosphatidylinositol 3-Kinases)
RN  - EC 2.7.10.1 (Receptor, Platelet-Derived Growth Factor beta)
SB  - IM
MH  - 3T3 Cells
MH  - *Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Animals
MH  - Becaplermin
MH  - Carrier Proteins/physiology
MH  - Cricetinae
MH  - DNA/*biosynthesis
MH  - Ecdysone/pharmacology
MH  - Insulin/*pharmacology
MH  - Insulin-Like Growth Factor I/*pharmacology
MH  - Mice
MH  - Microinjections
MH  - Molecular Sequence Data
MH  - Phosphatidylinositol 3-Kinases/physiology
MH  - Platelet-Derived Growth Factor/*pharmacology
MH  - Proto-Oncogene Proteins c-sis
MH  - Receptor, Platelet-Derived Growth Factor beta/physiology
MH  - src Homology Domains
EDAT- 2000/01/25 00:00
MHDA- 2000/01/25 00:01
CRDT- 2000/01/25 00:00
PHST- 2000/01/25 00:00 [pubmed]
PHST- 2000/01/25 00:01 [medline]
PHST- 2000/01/25 00:00 [entrez]
AID - 10.1038/sj.onc.1203253 [doi]
PST - ppublish
SO  - Oncogene. 2000 Jan 6;19(1):39-50. doi: 10.1038/sj.onc.1203253.