Identification of glycoproteins and proteins at synapses in the central nervous system.

Kelly, PT; Cotman, Carl W.

doi:10.1016/s0021-9258(17)32785-0

Cited by 146 publications

(22 citation statements)

References 31 publications

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“…We can now state that isolated SJs and PSDs contain a substantial amount of tubulin. Tubulin accounts for -7% of the total protein in SJ fractions and 14% in PSD fractions (17). Twodimensional electrophoresis reveals that SJ and PSD polypeptides comigrate with a-and/3-tubulin and that these spots share the same complexity (see Fig.…”

Section: Discussionmentioning

confidence: 96%

“…Actin has been shown to be associated with the postsynaptic region in situ by heavy meromyosinbinding studies (24). Other studies have suggested that a protein resembling actin in molecular weight is associated with isolated PSDs (9,17). Recently, Blomberg et al (6) have shown on the basis of antisera reactivity and amino acid composition that a polypeptide from dog PSDs is very similar to skeletal muscle a-actin.…”

Section: Discussionmentioning

confidence: 99%

“…Later, Westrum and Gray (34) observed microtubules associated with the PSD. Recent work in our laboratory (13,16,17,38) and others (30) have suggested that tubulin is present in isolated PSDs, but its identity and relationship to the major PSD protein remained uncertain. The data presented in this paper establish that the major PSD protein is distinct from tubulin and that SJ-and PSD-associated tubulin is, by these analyses, identical to cytoplasmic tubulin.…”

Section: Discussionmentioning

confidence: 99%

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Synaptic proteins. Characterization of tubulin and actin and identification of a distinct postsynaptic density polypeptide.

Kelly¹,

Cotman²

1978

The Journal of Cell Biology

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258

158

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The major proteins in isolated synaptic junctions (SJs) and postsynaptic densities (PSDs) have been compared to actin, tubulin, and the major neurofilament (NF) protein by two-dimensional gel electrophoresis and tryptic peptide map analysis.These studies show: (a) tubulin is present in SJ and PSD fractions and is identical to cytoplasmic tubulin, (b) actin in these fractions is very similar to the y-and/3-actin found predominantly in nonmuscle ceils, and (c) the major PSD protein is distinct from all other known fibrous proteins.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Synaptic proteins. Characterization of tubulin and actin and identification of a distinct postsynaptic density polypeptide.

Kelly¹,

Cotman²

1978

The Journal of Cell Biology

Self Cite

258

158

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“…SAP97, on the other hand, cannot associate with PSD-in the postsynaptic density, our findings can account, at least in part, for the biochemical observations of Cotman 95 and chapsyn-110 and is segregated from these proteins to presynaptic and axonal locations. The dis-and colleagues, who noted that PSD proteins exist in the brain as supramolecular aggregates cross-linked by tinctive multimerization behavior of SAP97 may reflect different mechanisms of ion channel organization in ax-disulfide bonds (Kelly and Cotman, 1977).…”

Section: Head-to-head Multimerization Of Psd-95mentioning

confidence: 99%

Disulfide-Linked Head-to-Head Multimerization in the Mechanism of Ion Channel Clustering by PSD-95

Hsueh

Kim

Sheng

1997

Neuron

196

166

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The PSD-95/SAP90 family of PDZ-containing proteins is directly involved in the clustering of specific ion channels at synapses. We report that channel clustering depends on a conserved N-terminal domain of PSD-95 that mediates multimerization and disulfide linkage of PSD-95 protomers. This N-terminal multimerization domain confers channel clustering activity on a single PDZ domain. Thus, channel clustering depends on aggregation of PDZ domains achieved by head-to-head multimerization of PSD-95, rather than by concatenation of PDZ domains in PSD-95 monomers. This mechanism predicts that PSD-95 can organize heterogeneous membrane protein clusters via differential binding specificities of its three PDZ domains. PSD-95 and its relative chapsyn-110 exist as disulfide-linked complexes in rat brain, consistent with head-to-head multimerization of these proteins in vivo.

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“…There is some evidence that these con A binding sites, at least in the postsynaptic membrane, are not free to diffuse in the plane of the membrane as are those in the extra-junctional membranes (Matus et al 1973 ;Cotman & Taylor 1974). It has been suggested that the transmembrane glyco proteins in the postsynaptic membrane at the synapse are anchored to the postsynaptic density and that this is the reason for their relative immobility (Matus et al 1973;Kelly et al 1976;Gurd 1977;Kelly & Cotman 1977).…”

Section: Discussionmentioning

confidence: 99%

Binding and uptake of concanavalin A into rat brain synaptosomes: evidence for synaptic vesicle recycling

1983

Proc. R. Soc. Lond. B.

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The specific binding of radioiodinated concanavalin A ( 125 I-con A) to rat brain synaptosomes was shown to be saturable. In the presence of excess con A binding was rapid and was completed within 5 min ( t 1/2 was 25 s) at 37°C, and at saturation the amount bound did not change over time. Under the electron microscope, concanavalin A-ferritin (con A-ft) bound to synaptosomes in two regions: in the extra-junctional plasma membrane and within the synaptic cleft of Gray type 1 and 2 synapses. Synaptosomes incubated with con A-ft at 37°C internalized bound lectin by endocytosis through coated pits. Endocytosis took place in the extra-junctional membrane, because it can occur before con A-ft has penetrated into the synaptic cleft, and continued for a considerable time (more than 30 min) after saturation of the receptor(s). Synaptic vesicles, which have at least two con A receptors on the internal aspect of their membranes, and cisternae, become labelled. When exocytosis was induced in synaptosomes by K + depolarizations, synaptic vesicle con A receptors became incorporated into the plasma membrane and were labelled with 125 I-con A causing a 2.5-fold increase in con A binding that was Ca 2+ dependent. These experiments thus provide evidence for the transient incorporation of synaptic vesicle membrane glycoproteins into the plasma membrane during transmitter release.

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Identification of glycoproteins and proteins at synapses in the central nervous system.

Cited by 146 publications

References 31 publications

Synaptic proteins. Characterization of tubulin and actin and identification of a distinct postsynaptic density polypeptide.

Synaptic proteins. Characterization of tubulin and actin and identification of a distinct postsynaptic density polypeptide.

Disulfide-Linked Head-to-Head Multimerization in the Mechanism of Ion Channel Clustering by PSD-95

Binding and uptake of concanavalin A into rat brain synaptosomes: evidence for synaptic vesicle recycling

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