Synapsins: Mosaics of shared and individual domains in a family of synaptic vesicle phosphoproteins

Thomas C. Südhof, Andrew J. Czernik, Hung Teh Kao, Kohji Takei, Patricia A. Johnston, Atsuko Horiuchi, Selma D. Kanazir, Michael A. Wagner, Mark S. Perin, Pietro De Camilli, Paul Greengard

Research output: Contribution to journalArticlepeer-review

151 Citations (Scopus)


Synapsins are neuronal phosphoproteins that coat synaptic vesicles, bind to the cytoskeleton, and are believed to function in the regulation of neurotransmitter release. Molecular cloning reveals that the synapsins comprise a family of four homologous proteins whose messenger RNA's are generated by differential splicing of transcripts from two genes. Each synapsin is a mosaic composed of homologous amino-terminal domains common to all synapsins and different combinations of distinct carboxyl-terminal domains. Immunocytochemical studies demonstrate that all four synapsins are widely distributed in nerve terminals, but that their relative amounts vary among different kinds of synapses. The structural diversity and differential distribution of the four synapsins suggest common and different roles of each in the integration of distinct signal transduction pathways that modulate neurotransmitter release in various types of neurons.

Original languageEnglish
Pages (from-to)1474-1480
Number of pages7
Issue number4925
Publication statusPublished - 1989
Externally publishedYes

ASJC Scopus subject areas

  • General


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