Cyclic Adenosine 3′:5′-Monophosphate-Stimulated Phosphorylation of Isolated Neurotubule Subunits | Zendy

David B. P. Goodman | Zendy; Howard Rasmussen | Zendy; Francis DiBella | Zendy; C. Earl Guthrow | Zendy

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Cyclic Adenosine 3′:5′-Monophosphate-Stimulated Phosphorylation of Isolated Neurotubule Subunits

Author(s) -

David B. P. Goodman,

Howard Rasmussen,

Francis DiBella,

C. Earl Guthrow

Publication year - 1970

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.67.2.652

Subject(s) - protein subunit , phosphorylation , protein kinase a , serine , biochemistry , adenosine , nucleotide , adenosine triphosphate , kinase , adenosine monophosphate , chemistry , biology , microbiology and biotechnology , biophysics , gene

The possible relationship between cyclic adenosine 3':5'-monophosphate (cAMP) and neurotubules in synaptic transmission has been explored. The neurotubular subunit protein from bovine cerebral cortex has been prepared. The addition of cAMP to this preparation in the presence of ATP stimulates the phosphorylation of serine residue(s) in the principal component of the preparation. The neurotubule subunit thus serves as a substrate for an intrinsic, cyclic nucleotide-dependent protein kinase closely associated with the neurotubule subunit. The significance of this finding is discussed in terms of a general model for cellular secretion involving microtubules, cyclic AMP, protein kinase, and calcium ion.

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