3j4r: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 9: Line 9:
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/AKA7G_RAT AKA7G_RAT] Probably targets cAMP-dependent protein kinase (PKA) to the cellular membrane or cytoskeletal structures. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium (By similarity). Isoform Delta may be involved in shuttling aquaporin-2 (AQP2) to the plasma membrane.[UniProtKB:Q9P0M2]<ref>PMID:15037626</ref>  
[https://www.uniprot.org/uniprot/AKA7G_RAT AKA7G_RAT] Probably targets cAMP-dependent protein kinase (PKA) to the cellular membrane or cytoskeletal structures. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium (By similarity). Isoform Delta may be involved in shuttling aquaporin-2 (AQP2) to the plasma membrane.[UniProtKB:Q9P0M2]<ref>PMID:15037626</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Anchoring proteins sequester kinases with their substrates to locally disseminate intracellular signals and avert indiscriminate transmission of these responses throughout the cell. Mechanistic understanding of this process is hampered by limited structural information on these macromolecular complexes. A-kinase anchoring proteins (AKAPs) spatially constrain phosphorylation by cAMP-dependent protein kinases (PKA). Electron microscopy and three-dimensional reconstructions of type-II PKA-AKAP18gamma complexes reveal hetero-pentameric assemblies that adopt a range of flexible tripartite configurations. Intrinsically disordered regions within each PKA regulatory subunit impart the molecular plasticity that affords an approximately 16 nanometer radius of motion to the associated catalytic subunits. Manipulating flexibility within the PKA holoenzyme augmented basal and cAMP responsive phosphorylation of AKAP-associated substrates. Cell-based analyses suggest that the catalytic subunit remains within type-II PKA-AKAP18gamma complexes upon cAMP elevation. We propose that the dynamic movement of kinase sub-structures, in concert with the static AKAP-regulatory subunit interface, generates a solid-state signaling microenvironment for substrate phosphorylation. DOI: http://dx.doi.org/10.7554/eLife.01319.001.
Intrinsic disorder within an AKAP-protein kinase A complex guides local substrate phosphorylation.,Smith FD, Reichow SL, Esseltine JL, Shi D, Langeberg LK, Scott JD, Gonen T Elife. 2013 Nov 5;2(0). pii: e01319. doi: 10.7554/eLife.01319. PMID:24192038<ref>PMID:24192038</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3j4r" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Latest revision as of 13:10, 21 February 2024

Pseudo-atomic model of the AKAP18-PKA Complex in a linear conformation derived from electron microscopyPseudo-atomic model of the AKAP18-PKA Complex in a linear conformation derived from electron microscopy

3j4r, resolution 35.00Å

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=3j4r&oldid=4065866"