Isoform-specific targeting of PKA to multivesicular bodies

Day, Michele E.; Gaietta, Guido; Sastri, Mira; Koller, Antonius; Mackey, Mason; Scott, John D.; Perkins, Guy; Ellisman, Mark H.; Taylor, Susan S.

doi:10.1083/jcb.201010034

Cited by 37 publications

(36 citation statements)

References 61 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It has previously been suggested that mTOR may be activated by deletion of Prkar1a and may directly interact with Prkar1a (24), although these data are somewhat controversial (25). Additionally, mTOR activation by TSH has been suggested to be, at least partly, due to PKA phosphorylation of the target of rapamycin complex 1 complex member PRAS40 (26).…”

Section: Discussionmentioning

confidence: 98%

Follicular Thyroid Cancers Demonstrate Dual Activation of PKA and mTOR as Modeled by Thyroid-Specific Deletion of Prkar1a and Pten in Mice

Pringle¹,

Vasko

et al. 2014

The Journal of Clinical Endocrinology &Amp; Metabolism

View full text Add to dashboard Cite

These data imply that the protein kinase A and mTOR signaling cascades are important for the development of follicular thyroid carcinogenesis and may suggest new targets for therapeutic intervention. Mouse models paralleling the development of the stages of human FTC should provide important new tools for understanding the mechanisms of FTC development and progression and for evaluating new therapeutics.

show abstract

Section: Discussionmentioning

confidence: 98%

Follicular Thyroid Cancers Demonstrate Dual Activation of PKA and mTOR as Modeled by Thyroid-Specific Deletion of Prkar1a and Pten in Mice

Pringle¹,

Vasko

et al. 2014

The Journal of Clinical Endocrinology &Amp; Metabolism

View full text Add to dashboard Cite

show abstract

“…In mammalian cells, the MVBs play a positive role in activating Wnt signaling, by sequestering the inhibitor (GSK3) within the ILVs [44]. In another example, the free RIα subunit of cPKA is sequestered onto the surface of MVB's by AKAP11 in a cAMP dependent manner [42]. Finally, the integrity of the late endosomes is crucial for amino-acid and insulin stimulated mTOR signaling [43].…”

Section: Discussionmentioning

confidence: 99%

“…Endosomes are known to serve functions beyond cargo sorting. Recent findings suggest that endosomal compartments additionally function as signaling anchors/platforms, integrating membrane trafficking and intracellular signal transduction [42], [43], [44], [45], [46], [47].…”

Section: Introductionmentioning

confidence: 99%

The Late Endosomal HOPS Complex Anchors Active G-Protein Signaling Essential for Pathogenesis in Magnaporthe oryzae

et al. 2013

View full text Add to dashboard Cite

In Magnaporthe oryzae, the causal ascomycete of the devastating rice blast disease, the conidial germ tube tip must sense and respond to a wide array of requisite cues from the host in order to switch from polarized to isotropic growth, ultimately forming the dome-shaped infection cell known as the appressorium. Although the role for G-protein mediated Cyclic AMP signaling in appressorium formation was first identified almost two decades ago, little is known about the spatio-temporal dynamics of the cascade and how the signal is transmitted through the intracellular network during cell growth and morphogenesis. In this study, we demonstrate that the late endosomal compartments, comprising of a PI3P-rich (Phosphatidylinositol 3-phosphate) highly dynamic tubulo-vesicular network, scaffold active MagA/GαS, Rgs1 (a GAP for MagA), Adenylate cyclase and Pth11 (a non-canonical GPCR) in the likely absence of AKAP-like anchors during early pathogenic development in M. oryzae. Loss of HOPS component Vps39 and consequently the late endosomal function caused a disruption of adenylate cyclase localization, cAMP signaling and appressorium formation. Remarkably, exogenous cAMP rescued the appressorium formation defects associated with VPS39 deletion in M. oryzae. We propose that sequestration of key G-protein signaling components on dynamic late endosomes and/or endolysosomes, provides an effective molecular means to compartmentalize and control the spatio-temporal activation and rapid downregulation (likely via vacuolar degradation) of cAMP signaling amidst changing cellular geometry during pathogenic development in M. oryzae.

show abstract

“…Although RI subunits were typically found to be more diffuse in the cytoplasm than RII subunits, they could also be recruited in a more dynamic way as evidenced by the migration of RI to the cap site in activated lymphocytes (45) and following treatment of cardiac myocytes with H 2 O 2 (46). Furthermore, it was shown that overexpressed RI␣ and C subunits were still associated with AKAP220 even though they were diffuse in the cytoplasm; however, targeting of the RI␣ subunit to multivesicular bodies only occurred upon activation of the complex (47).…”

Section: Discussionmentioning

confidence: 99%

A Small Novel A-Kinase Anchoring Protein (AKAP) That Localizes Specifically Protein Kinase A-Regulatory Subunit I (PKA-RI) to the Plasma Membrane

Burgers

Margarucci

et al. 2012

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

Isoform-specific targeting of PKA to multivesicular bodies

Abstract: PKA RIα subunit is localized to MVBs by the A-kinase–anchoring protein AKAP11 when disassociated from the PKA catalytic subunit.

Cited by 37 publications

References 61 publications

Follicular Thyroid Cancers Demonstrate Dual Activation of PKA and mTOR as Modeled by Thyroid-Specific Deletion of Prkar1a and Pten in Mice

Follicular Thyroid Cancers Demonstrate Dual Activation of PKA and mTOR as Modeled by Thyroid-Specific Deletion of Prkar1a and Pten in Mice

The Late Endosomal HOPS Complex Anchors Active G-Protein Signaling Essential for Pathogenesis in Magnaporthe oryzae

A Small Novel A-Kinase Anchoring Protein (AKAP) That Localizes Specifically Protein Kinase A-Regulatory Subunit I (PKA-RI) to the Plasma Membrane

Contact Info

Product

Resources

About