PMID- 10469599
OWN - NLM
STAT- MEDLINE
DCOM- 19991223
LR  - 20131121
IS  - 0960-9822 (Print)
IS  - 0960-9822 (Linking)
VI  - 9
IP  - 16
DP  - 1999 Aug 26
TI  - SHPS-1 is a scaffold for assembling distinct adhesion-regulated multi-protein
      complexes in macrophages.
PG  - 927-30
AB  - Inhibitory immunoreceptors downregulate signaling by recruiting Src homology 2
      (SH2) domain-containing tyrosine and/or lipid phosphatases to activating receptor
      complexes [1]. There are indications that some inhibitory receptors might also
      perform other functions [2] [3]. In adherent macrophages, two inhibitory
      receptors, SHPS-1 and PIR-B, are the major proteins binding to the tyrosine
      phosphatase SHP-1. SHPS-1 also associates with two tyrosine-phosphorylated
      proteins (pp55 and pp130) and a protein tyrosine kinase [4]. Here, we have
      identified pp55 and pp130 as the adaptor molecules SKAP55hom/R
      (Src-kinase-associated protein of 55 kDa homologue) and FYB/SLAP-130 (Fyn-binding
      protein/SLP-76-associated protein of 130 kDa), respectively, and the tyrosine
      kinase activity as PYK2. Two distinct SHPS-1 complexes were formed, one
      containing SKAP55hom/R and FYB/SLAP-130, and the other containing PYK2.
      Recruitment of FYB/SLAP-130 to SHPS-1 required SKAP55hom/R, whereas PYK2
      associated with SHPS-1 independently. Formation of both complexes was independent
      of SHP-1 and tyrosine phosphorylation of SHPS-1. Finally, tyrosine
      phosphorylation of members of the SHPS-1 complexes was regulated by
      integrin-mediated adhesion. Thus, SHPS-1 provides a scaffold for the assembly of 
      multi-protein complexes that might both transmit adhesion-regulated signals and
      help terminate such signals through SHP-1-directed dephosphorylation. Other
      inhibitory immunoreceptors might have similar scaffold-like functions.
FAU - Timms, J F
AU  - Timms JF
AD  - Cancer Biology Program, Division of Hematology-Oncology, Department of Medicine, 
      Beth Israel Deaconess Medical Center, Harvard Medical School, Boston,
      Massachusetts 02215, USA.
FAU - Swanson, K D
AU  - Swanson KD
FAU - Marie-Cardine, A
AU  - Marie-Cardine A
FAU - Raab, M
AU  - Raab M
FAU - Rudd, C E
AU  - Rudd CE
FAU - Schraven, B
AU  - Schraven B
FAU - Neel, B G
AU  - Neel BG
LA  - eng
GR  - P01 DK50654/DK/NIDDK NIH HHS/United States
GR  - T32 HL07623/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Curr Biol
JT  - Current biology : CB
JID - 9107782
RN  - 0 (Antigens, Differentiation)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Neural Cell Adhesion Molecule L1)
RN  - 0 (Neural Cell Adhesion Molecules)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (Ptpns1 protein, mouse)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (Sulfones)
RN  - 0 (nucleolar phosphoprotein p130)
RN  - 149970-64-9
      (5'-O-(((2-decanoylamino-3-phenylpropyloxycarbonyl)amino)sulfonyl)uridine)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (Focal Adhesion Kinase 1)
RN  - EC 2.7.10.2 (Focal Adhesion Kinase 2)
RN  - EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (Ptk2 protein, mouse)
RN  - EC 2.7.10.2 (Ptk2b protein, mouse)
RN  - EC 3.2.1.96 (Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase)
RN  - WHI7HQ7H85 (Uridine)
SB  - IM
MH  - Animals
MH  - *Antigens, Differentiation
MH  - Bone Marrow Cells/*chemistry
MH  - COS Cells
MH  - Cell Adhesion
MH  - Cell Adhesion Molecules/analysis/metabolism
MH  - Focal Adhesion Kinase 1
MH  - Focal Adhesion Kinase 2
MH  - Focal Adhesion Protein-Tyrosine Kinases
MH  - Immunoblotting
MH  - Macrophages/*chemistry/drug effects
MH  - Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase/pharmacology
MH  - Membrane Glycoproteins/*metabolism
MH  - Mice
MH  - Mice, Mutant Strains
MH  - *Neural Cell Adhesion Molecule L1
MH  - Neural Cell Adhesion Molecules/*metabolism
MH  - Nuclear Proteins/analysis/metabolism
MH  - Phosphoproteins/analysis/metabolism
MH  - *Protein Folding
MH  - Protein-Tyrosine Kinases/analysis/metabolism
MH  - *Receptors, Immunologic
MH  - Sulfones/analysis/metabolism
MH  - Uridine/analogs & derivatives/analysis/metabolism
EDAT- 1999/09/02 00:00
MHDA- 1999/09/02 00:01
CRDT- 1999/09/02 00:00
PHST- 1999/09/02 00:00 [pubmed]
PHST- 1999/09/02 00:01 [medline]
PHST- 1999/09/02 00:00 [entrez]
AID - S0960-9822(99)80401-1 [pii]
PST - ppublish
SO  - Curr Biol. 1999 Aug 26;9(16):927-30.