PMID- 7891172
OWN - NLM
STAT- MEDLINE
DCOM- 19950417
LR  - 20191231
IS  - 0270-6474 (Print)
IS  - 1529-2401 (Electronic)
IS  - 0270-6474 (Linking)
VI  - 15
IP  - 3 Pt 2
DP  - 1995 Mar
TI  - Molecular characterization and spatial distribution of SAP97, a novel presynaptic 
      protein homologous to SAP90 and the Drosophila discs-large tumor suppressor 
      protein.
PG  - 2354-66
AB  - Synapses are highly specialized sites of cell-cell contact involved in signal 
      transfer. The molecular mechanisms modulating the assembly and stability of 
      synapses are unknown. We previously reported the identification of a 90 kDa 
      synapse-associated protein, SAP90, that is localized at the presynaptic termini 
      of inhibitory GABAergic synapses. SAP90 is a mosaic protein composed of three 90 
      amino acid residue repeats, an SH3 domain and a region homologous to guanylate 
      kinases. SAP90 shares domain specific homology with a family of proteins involved 
      in the assembly and possibly stability of sites of cell contact. These include 
      the product of the lethal(1) discs-large-1 (dlgA) tumor suppressor gene and the 
      zonula occludens proteins ZO-1, ZO-2. The further characterization of cDNA clones 
      encoding components of synaptic junctions has lead to the identification of a 97 
      kDa protein, called SAP97, that exhibits a strong overall sequence similarity to 
      SAP90. The present study was undertaken to determine the spatial distribution of 
      SAP97, and to reveal further clues to the possible roles of these proteins in 
      synapses. Light and immunoelectron microscopic analysis of the rat hippocampal 
      formation revealed that SAP97 is localized in the presynaptic nerve termini of 
      excitatory synapses. In other brain regions, SAP97 is found in and along bundles 
      of unmyelinated axons. SAP97 is not restricted to the CNS, but is also present at 
      the basal lateral membrane between a variety of epithelial cells. In cultured T84 
      cells, it is restricted to the cytoplasmic surface of the plasma membranes 
      between adjacent cells, but not at the edges of cells lacking cell-cell contact 
      suggesting a role for SAP97 in cell adhesion. These data suggest that members of 
      the SAP90/SAP97 subfamily may be involved in the site specific assembly, 
      stability or functions of membrane specialization at sites of cell-cell contact.
FAU - Muller, B M
AU  - Muller BM
AD  - Center for Molecular Neurobiology, University of Hamburg, Germany.
FAU - Kistner, U
AU  - Kistner U
FAU - Veh, R W
AU  - Veh RW
FAU - Cases-Langhoff, C
AU  - Cases-Langhoff C
FAU - Becker, B
AU  - Becker B
FAU - Gundelfinger, E D
AU  - Gundelfinger ED
FAU - Garner, C C
AU  - Garner CC
LA  - eng
SI  - GENBANK/U14950
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Neurosci
JT  - The Journal of neuroscience : the official journal of the Society for 
      Neuroscience
JID - 8102140
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (DNA, Complementary)
RN  - 0 (Dlg1 protein, rat)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Insect Hormones)
RN  - 0 (Membrane Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (SAP90-PSD95 Associated Proteins)
RN  - 0 (Tumor Suppressor Proteins)
RN  - 143513-41-1 (dlg1 protein, Drosophila)
SB  - IM
GS  - dlg-A
MH  - Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Animals
MH  - Axons/chemistry
MH  - Base Sequence
MH  - *Brain Chemistry
MH  - Cerebellum/metabolism/ultrastructure
MH  - Cloning, Molecular
MH  - DNA, Complementary/genetics
MH  - *Drosophila Proteins
MH  - Drosophila melanogaster/chemistry/genetics
MH  - Genes, Insect
MH  - Genes, Tumor Suppressor
MH  - Hippocampus/metabolism/ultrastructure
MH  - In Situ Hybridization
MH  - Insect Hormones/*chemistry
MH  - Intercellular Junctions/chemistry
MH  - Intestinal Mucosa/chemistry/cytology
MH  - Membrane Proteins
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/analysis/*chemistry/genetics
MH  - Organ Specificity
MH  - Polymorphism, Restriction Fragment Length
MH  - RNA, Messenger/analysis
MH  - Rats
MH  - SAP90-PSD95 Associated Proteins
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Signal Transduction
MH  - Synapses/*chemistry
MH  - *Tumor Suppressor Proteins
PMC - PMC6578138
EDAT- 1995/03/01 00:00
MHDA- 1995/03/01 00:01
PMCR- 1995/09/01
CRDT- 1995/03/01 00:00
PHST- 1995/03/01 00:00 [pubmed]
PHST- 1995/03/01 00:01 [medline]
PHST- 1995/03/01 00:00 [entrez]
PHST- 1995/09/01 00:00 [pmc-release]
AID - 10.1523/JNEUROSCI.15-03-02354.1995 [doi]
PST - ppublish
SO  - J Neurosci. 1995 Mar;15(3 Pt 2):2354-66. doi: 10.1523/JNEUROSCI.15-03-02354.1995.