Results 171 to 180 of about 6,190 (209)
AKAP-Lbc: A molecular scaffold for the integration of cyclic AMP and Rho transduction pathways
A Kinase-anchoring proteins (AKAPs) are a family of functionally related proteins involved in the targeting of the PKA holoenzyme towards specific physiological substrates. We have recently identified a novel anchoring protein expressed in cardiomyocytes,
Dario Diviani
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AKAP-Lbc mediates protection against doxorubicin-induced cardiomyocyte toxicity
Doxorubicin (DOX) is a chemotherapic agent that is widely used to treat hematological and solid tumors. Despite its efficacy, DOX displays significant cardiac toxicity associated with cardiomyocytes death and heart failure.
Dario Diviani
exaly +2 more sources
The C-terminus of the long AKAP13 isoform (AKAP-Lbc) is critical for development of compensatory cardiac hypertrophy [PDF]
The objective of this study was to determine the role of A-Kinase Anchoring Protein (AKAP)-Lbc in the development of heart failure, by investigating AKAP-Lbc-protein kinase D1 (PKD1) signaling in vivo in cardiac hypertrophy.
Kathrin Banach +2 more
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Anchoring of both PKA and 14‐3‐3 inhibits the Rho‐GEF activity of the AKAP‐Lbc signaling complex
A-kinase anchoring proteins (AKAPs) target the cAMP-regulated protein kinase (PKA) to its physiological substrates. We recently identified a novel anchoring protein, called AKAP-Lbc, which functions as a PKA-targeting protein as well as a guanine ...
Dario Diviani
exaly +2 more sources
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AKAP Mediated Signal Transduction
Annual Review of Pharmacology and Toxicology, 2002Compartmentalization 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.
Jennifer J Carlisle, Michel +1 more
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AKAPs: from structure to function
Trends in Cell Biology, 1999Compartmentalization of signalling molecules through association with anchoring proteins ensures specificity in signal transduction by placing enzymes close to their appropriate effectors and substrates. For example, 'A-kinase anchoring proteins' (AKAPs) bind to the regulatory subunit of cAMP-dependent protein kinase (PKA) to direct the kinase to ...
M, Colledge, J D, Scott
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AKAPs as Antiarrhythmic Targets?
2006Phosphorylation of ion channels plays a critical role in the modulation and amplification of biophysical signals. Kinases and phosphatases have broad substrate recognition sequences. Therefore, the targeting of kinases and phosphatases to specific sites enhances the regulation of diverse signaling events.
S O, Marx, J, Kurokawa
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Potential therapeutic applications of AKAP disrupting peptides
Clinical Science, 2020Abstract The 3′–5′-cyclic adenosine monophosphate (cAMP)/PKA pathway represents a major target for pharmacological intervention in multiple disease conditions. Although the last decade saw the concept of highly compartmentalized cAMP/PKA signaling consolidating, current means for the manipulation of this pathway still do not allow to ...
Alessandra, Murabito +3 more
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AKAP7γ is a nuclear RI-binding AKAP
Biochemical and Biophysical Research Communications, 2003Spatial regulation of protein kinase A (PKA) is accomplished by its sequestration via A-kinase anchor proteins (AKAPs). PKA activity is critical for mammalian oocyte development, suggesting that PKA must be appropriately positioned in these large cells. A screen for AKAPs in oocytes identified AKAP7gamma, an AKAP originally found in pancreas. Yeast two-
Rebecca L, Brown +3 more
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A Gα12-specific Binding Domain in AKAP-Lbc and p114RhoGEF
AKAP-Lbc is a Rho-activating guanine nucleotide exchange factor (RhoGEF) important in heart development and pro-fibrotic signaling in cardiomyocytes. Heterotrimeric G proteins of the G12/13 subfamily, comprising Gα12 and Gα13, are well characterized as stimulating a specialized group of RhoGEFs through interaction with their RGS-homology (RH) domain ...
Thomas E Meigs
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