October 1, 1989Journal of Biological ChemistryOpen Access

Functional Characterization of cAMP-binding Mutations in Type I Protein Kinase

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Population

Recombinant wild type RI, B1 mutant, B2 mutant, mouse AtT20 pituitary cells, and human JEG-3 choriocarcinoma…

Comparison

Expression of B1 or B2 mutant RI subunits vs Wild type RI subunit

Design

Preclinical

Authors

LCL A CorrellSalk Institute for Biological Studies TWTerry A. WoodfordHoward Hughes Medical Institute JCJackie D. CorbinDartmouth College

Discussion

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Implication

B-site PKA mutations may repress activity in vivo; leaves open relevance to human cAMP signaling disorders.

Structured PICO

Population

Recombinant wild type RI, B1 mutant, B2 mutant, mouse AtT20 pituitary cells, and human JEG-3 choriocarcinoma cells

Intervention

Expression of B1 or B2 mutant RI subunits

Comparator

Wild type RI subunit

Outcome

Rate of dissociation of cAMP from RI, cAMP-mediated activation of holoenzyme, and inducibility of cAMP-responsive genessurrogate

The Gly to Asp mutation at amino acid 324 completely blocks cAMP binding to site B, whereas the Arg to His mutation at position 332 causes a more subtle alteration, both resulting in dominant repression of cAMP-dependent protein kinase activity.

Cite This Study

Correll et al. (1989) studied this question.

synapsesocial.com/papers/6a7cae024ec837fd6928a708 https://doi.org/10.1016/s0021-9258(19)84758-0

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Functional Characterization of cAMP-binding Mutations in Type I Protein Kinase

Discussion

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Implication

Structured PICO

Cite This Study

Functional Characterization of cAMP-binding Mutations in Type I Protein Kinase

Discussion

Member takes

Implication

Structured PICO

Cite This Study

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