AKAP350 at the Golgi Apparatus

Shanks, Ryan A.; Steadman, Brent T.; Schmidt, P. Henry; Goldenring, James R.

doi:10.1074/jbc.m203307200

Cited by 39 publications

(16 citation statements)

References 19 publications

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“…Identified binding partners for CLICs include a variety of proteins involved in membrane traffic and the cytoskeleton. [37][38][39][40][41] Undoubtedly recruitment of components of the membrane fusion machinery and dynamic regulation of the cytoskeleton must play an important roles in endothelial tubulogenesis. Whether CLIC4 contributes through these mechanism remains to be explored.…”

Section: Discussionmentioning

confidence: 99%

Chloride Intracellular Channel Protein-4 Functions in Angiogenesis by Supporting Acidification of Vacuoles Along the Intracellular Tubulogenic Pathway

Ulmasov

Bruno

Gordon

et al. 2009

The American Journal of Pathology

118

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Endothelial cells form capillary tubes through the process of intracellular tubulogenesis. Chloride intracellular channel (CLIC) family proteins have been previously implicated in intracellular tubulogenesis, but their specific role has not been defined. In this study, we show that disruption of the Clic4 gene in mice results in defective angiogenesis in vivo as reflected in a Matrigel plug angiogenesis assay. An angiogenesis defect is also apparent in the retina, both in the decreased spontaneous development of retinal vasculature of unstressed mice and in the dramatically decreased angiogenic response of retinal vessels to an oxygen toxicity challenge. We found that endothelial cells derived from Clic4 ؊/؊ mice demonstrated impaired tubulogenesis in three-dimensional fibrin gels compared with cells derived from wild-type mice. Furthermore, we found that tubulogenesis of wildtype cells in culture was inhibited by both an inhibitor of CLICs and an inhibitor of the vacuolar proton ATPase. Finally, we showed that vacuoles along the endothelial tubulogenesis pathway are acidic in wildtype cells, and that vacuolar acidification is impaired in Clic4 ؊/؊ cells while lysosomal acidification is intact. We conclude that CLIC4 plays a critical role in angiogenesis by supporting acidification of vacuoles along the cell-hollowing tubulogenic pathway.

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Section: Discussionmentioning

confidence: 99%

Chloride Intracellular Channel Protein-4 Functions in Angiogenesis by Supporting Acidification of Vacuoles Along the Intracellular Tubulogenic Pathway

Ulmasov

Bruno

Gordon

et al. 2009

The American Journal of Pathology

118

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“…Two forms of the PKA holoenzyme are found inside cells, depending on the R subunit: type I is mostly cytoplasmic, and type II is found associated with specific cellular structures and organelles. PKA type II has been found, among other intracellular locations, in endosomal and Golgi membranes (Griffiths et al, 1990;McCahill et al, 2005;Shanks et al, 2002;Tasken et al, 2001;Witczak et al, 1999) and in autophagosomal organelles (Kotoulas et al, 2003). This enzyme is bound to non-enzymatic scaffolding proteins termed A-kinase anchoring proteins (AKAPs).…”

Section: Introductionmentioning

confidence: 99%

cAMP synthesis and degradation by phagosomes regulate actin assembly and fusion events: consequences for mycobacteria

Kalamidas

Kuehnel

Peyron

et al. 2006

Journal of Cell Science

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We showed recently that actin assembly by phagosomal membranes facilitates fusion with late endocytic organelles in macrophages. Moreover, lipids that induced phagosomal actin also stimulated this fusion process. In macrophages infected with pathogenic mycobacteria actin-stimulatory lipids led to an increase in pathogen destruction, whereas inhibitors facilitated their growth. A model was proposed whereby phagosomal membrane actin assembly provides tracks for lysosomes to move towards phagosomes, thereby facilitating fusion. Here, we investigated how cAMP affected phagosomal actin assembly in vitro, and phagosomal actin, acidification and late fusion events in J774 macrophages. Latex bead phagosomes are shown to possess adenylyl cyclase activity, which synthesizes cAMP, and phosphodiesterase activity, which degrades cAMP. The system is regulated by protein kinase A (PKA). Increasing cAMP levels inhibited, whereas decreasing cAMP levels stimulated, actin assembly in vitro and within cells. Increasing cAMP levels also inhibited phagosome-lysosome fusion and acidification in cells, whereas reducing cAMP had the opposite effect. High cAMP levels induced an increase in intraphagosomal growth in macrophages of both the non-pathogenic Mycobacterium smegmatis and the pathogenic Mycobacterium tuberculosis, whereas low cAMP levels or inhibition of PKA correlated with increased bacterial destruction. We argue that the phagosome cAMP-PKA system behaves as a molecular switch that regulates phagosome actin and maturation in macrophages.

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“…Both RI and RII colocalize with MAP2D in the Golgi matrix, as evidenced by confocal microscopy. However, there are other AKAPs associated with the Golgi apparatus that appear to preferentially bind either RII, such as MTG (81), an unidentified 85-kDa AKAP (57), and AKAP 350 (70) or RI, such as PAP7 (19). Thus, RI and RII localized to the Golgi are not exclusively bound to MAP2D.…”

Section: Map2d Plays a Functional Role In Lh Receptormentioning

confidence: 99%

Neuronal Microtubule-associated Protein 2D Is a Dual A-kinase Anchoring Protein Expressed in Rat Ovarian Granulosa Cells

Salvador

Flynn

Ávila

et al. 2004

Journal of Biological Chemistry

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Ovarian follicles house the oocyte and, upon maturation, produce steroid and protein hormones that regulate uterine receptivity and the reproductive axis. Follicles exist in a relatively dormant, preantral (PA) 1 state until they are recruited to grow and differentiate to a preovulatory (PO) phenotype by the pituitary hormone follicle-stimulating hormone (FSH) (1, 2). Maturation of follicles to a PO phenotype involves not only proliferation but also differentiation of the enclosed granulosa cells. FSH triggers these events by binding to its G-proteincoupled receptor, located exclusively on granulosa cells in female mammals, and activating adenylyl cyclase, which converts ATP to cAMP. cAMP then acts as a second messenger primarily by activating protein kinase A (PKA) (3). PKA is a tetrameric enzyme that consists of a dimeric regulatory (R) subunit and two catalytic subunits (4). Upon binding of cAMP to the R subunits, a conformational change occurs that allows for dissociation of the active catalytic subunits, which can then phosphorylate neighboring substrates. Two classes of PKA holoenzymes, PKA I and PKA II, exist based on the association of two possible RI subunits (RI␣ and RI␤) or two possible RII subunits (RII␣ and RII␤) with four possible catalytic subunits (C␣, C␤1, C␤2, and C␥) (5). In rat granulosa cells of PA and PO follicles, PKA II␣ and PKA II␤ are the predominant PKA isoforms present, whereas less than 5% of PKA holoenzyme activity is contributed by PKA I␣ (6 -8).The specificity of PKA action is accomplished by the targeting of PKA to specific cellular locales by virtue of its binding to a growing family of A-kinase anchoring proteins (AKAPs). Most known AKAPs anchor RII and exhibit at least a 100-fold lower affinity for RI (9). RII subunits of PKA bind with nanomolar affinity to AKAPs (5, 10). The domain on the AKAP responsible for RII binding comprises an amphipathic helix that binds to the N termini of the RII dimer (11). A growing number of "dual" AKAPs have been identified, although they still exhibit higher affinity for RII over . Recent reports, however, indicate that some AKAPs can preferentially bind . AKAPs anchor PKA to specific cellular locations, such as the actin cytoskeleton (20, 21), plasma membrane (22), mitochondria (23, 24), Golgi apparatus (25), centrosome (26), and nuclear envelope (27). The localization of PKA to distinct regions within the cell is generally thought to allow for both specific and efficient substrate phosphorylation in response to a specific stimulus (28).FSH receptor signaling in PA granulosa cells stimulates the PKA-dependent phosphorylation of a number of signaling intermediates including histone H3 (29), cAMP-response element-binding protein (CREB) (30,31), and an extracellular regulated kinase (ERK)-protein-tyrosine phosphatase that

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AKAP350 at the Golgi Apparatus

Cited by 39 publications

References 19 publications

Chloride Intracellular Channel Protein-4 Functions in Angiogenesis by Supporting Acidification of Vacuoles Along the Intracellular Tubulogenic Pathway

Chloride Intracellular Channel Protein-4 Functions in Angiogenesis by Supporting Acidification of Vacuoles Along the Intracellular Tubulogenic Pathway

cAMP synthesis and degradation by phagosomes regulate actin assembly and fusion events: consequences for mycobacteria

Neuronal Microtubule-associated Protein 2D Is a Dual A-kinase Anchoring Protein Expressed in Rat Ovarian Granulosa Cells

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