The DOI matches its Crossref record; 118 of the 118 references it cites were found in a registry or an index.
AKAP Mediated Signal Transduction
Abstract
Compartmentalization of cyclic AMP-dependent protein kinase (PKA) is achieved through association with A-kinase anchoring proteins (AKAPs). AKAPs are a group of structurally diverse proteins with the common function of binding to the regulatory subunit of PKA and confining the holoenzyme to discrete locations within the cell. This mode of regulation ensures that PKA is exposed to isolated cAMP gradients, which allows for efficient catalytic activation and accurate substrate selection. Several AKAPs coordinate multiple members of signaling cascades, effectively assembling upstream activators and downstream effectors within the same macromolecular complex. Consequently, AKAPs may serve as points of integration for numerous signaling pathways. This review details the most recent advances in our understanding of the various biological functions dependent upon AKAP-anchored signaling complexes.
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Cited by
Protein kinase CK2: structure, regulation and role in cellular decisions of life and death
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Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
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Specificity in Signal Transduction
Pawson, T. (2004) · Cell · doi:10.1016/s0092-8674(03)01077-8 · Cited by 816
Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm
NEWTON, A. C. (2003) · Biochemical Journal · doi:10.1042/bj20021626 · Cited by 798
Metadata
- Authors
- Michel, J. J. C., & Scott, J. D.
- Venue
- Annual Review of Pharmacology and Toxicology
- Publisher
- Annual Reviews
- Published
- 2002-04
- Volume
- 42
- Issue
- 1
- Pages
- 235-257
- ISSN
- 0362-1642 (ISSN-L)
- 1545-4304
- OpenAlex
- W2144796569
- Cited by
- 342
- References
- 118
- FWCI
- 2.50
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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