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Synapsin I is a spectrin-binding protein immunologically related to erythrocyte protein 4.1

Nature volume 315, pages 410–413 (1985)Cite this article

Abstract

The membrane-associated cytoskeleton is considered to be the apparatus by which cells regulate the properties of their plasma membranes, although recent evidence has indicated additional roles for the proteins of this structure, including an involvement in intracellular transport and exocytosis (see refs 1–3 for review). Of the membrane skeletal proteins, to date only spectrin (fodrin) and ankyrin have been purified and characterized from non-erythroid sources. Protein 4.1 in the red cell is a spectrin-binding protein4,5 that enhances the binding of spectrin to actin4,6,7 and can apparently bind to at least one transmembrane protein8–10 Immunoreactive forms of 4.1 have been detected in several cell types, including brain11–14. Here we report the purification of brain 4.1 on the basis of its cross-reactivity with erythrocyte 4.1 and spectrin-binding activity. We further show that brain 4.1 is identical to the synaptic vesicle protein, synapsin I, one of the brain's major substrates for cyclic AMP and Ca2+–calmodulin-dependent kinases15,16. Spectrin and synapsin are present in brain homogenates in an ∼1:1 molar ratio. Although synapsin I has been implicated in synaptic transmission, no activity has been previously ascribed to it.

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Authors and Affiliations

  1. Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205, USA

    Anthony J. Baines & Vann Bennett

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  1. Anthony J. Baines
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  2. Vann Bennett
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Baines, A., Bennett, V. Synapsin I is a spectrin-binding protein immunologically related to erythrocyte protein 4.1. Nature 315, 410–413 (1985). https://doi.org/10.1038/315410a0

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