AKAP350 Interaction with cdc42 Interacting Protein 4 at the Golgi Apparatus

Larocca, M. Cecilia; Shanks, Ryan A.; Tian, Lei; Nelson, David L.; Stewart, Dawn; Goldenring, James R.

doi:10.1091/mbc.e03-10-0757

Cited by 60 publications

(77 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although common themes emerge throughout the F-BAR family-tubulation of the membrane, Phosphoregulation may be a means by which several members of the F-BAR scaffolding family and BAR superfamily are spatially and temporally controlled. Several F-BAR proteins are phosphorylated in vivo, including PACSIN/syndapin, 43 PSTPIP, 40 CIP4, 44 and Hof1. 20 Importantly, phosphorylation of these proteins also appears to be inhibitory, as phosphorylation blocks the interaction of PSTPIP1 with WASP 45 and phosphorylation of Hof1 leads to ubiquitin-mediated degradation.…”

Section: F-bar Family Regulationmentioning

confidence: 99%

Setting the F-BAR: Functions and regulation of the F-BAR protein family

Roberts-Galbraith¹,

Gould²

2010

Cell Cycle

View full text Add to dashboard Cite

Section: F-bar Family Regulationmentioning

confidence: 99%

Setting the F-BAR: Functions and regulation of the F-BAR protein family

Roberts-Galbraith¹,

Gould²

2010

Cell Cycle

View full text Add to dashboard Cite

“…AKAP450 is located at the GA and MTOC and controls centrosome function during cell cycle, 17 Golgi organization, 35 and microtubule nucleation 22 in adherent epithelial cells and fibroblasts. However, in T lymphocytes, AKAP450 targeting with the C-term AKAP450-GFP construct did not significantly affect the cell-cycle progression and Golgi structure/organization by confocal level (supplemental Figures 1B, 4).…”

Section: Suppression Of Akap450 Function Prevents Mtoc Translocation mentioning

confidence: 99%

“…In addition to its role in IS formation, AKAP450 might also regulate GA function. AKAP450 is localized at the Golgi complex, 21,35 and its role in nucleating microtubules at the cis face of the Golgi might be important for MTOC/GA translocation and function. 22 The diminished release of IL-2 by AKAP450-disrupted T cells during the formation of the IS could therefore be the result of the defective MTOC/GA translocation observed in these cells.…”

mentioning

confidence: 99%

Integrin and CD3/TCR activation are regulated by the scaffold protein AKAP450

Robles‐Valero

Martín-Cófreces

Lamana

et al. 2010

Blood

View full text Add to dashboard Cite

IntroductionDuring the process of antigen recognition by T cells, structural and spatial changes take place at the immune synapse (IS) formed at the contact with antigen-presenting cells (APCs), involving various recognition and signaling molecules as well as cytoskeletal components. In T cells, the IS contains a central supramolecular activation cluster (c-SMAC), which includes the T-cell receptor (TCR)/CD3 complex and various costimulatory receptors, and a peripheral ring (p-SMAC) where molecules, such as lymphocyte functionassociated antigen 1 (LFA-1) and talin, localize. [1][2][3] The formation of the IS is associated with a substantial remodeling of the actin and tubulin cytoskeleton. 4,5 An early event on antigen recognition is the translocation of the centrosome, or microtubule-organizing center (MTOC), and the associated Golgi apparatus (GA) and secretory vesicles toward the nascent IS, bringing them in close apposition with the APCs. 6 This process provides the basis for polarized secretion of various molecules by the T cell, thus favoring controlled communication with the APCs. 7,8 Moreover, during asymmetric T lymphocyte division, stable orientation of original MTOC is essential to initiate differentiation associated with the adaptive immune responses of T cells. 9 The physical proximity of the MTOC and GA in mammalian cells is accompanied by a functional link between these organelles. The Golgi protein Golgi Matrix 130 (GM130) has recently been implicated in the regulation of MTOC morphology and function, 10,11 and Golgi Reassembly Stacking protein 65 (GRASP65) is another Golgi-associated protein required for MTOC/GA remodeling and positioning. 12 The scaffolding protein CG-NAP (centrosome and Golgi localized protein kinase N-associated protein), also known as A-kinase anchoring protein-9 (AKAP9), AKAP450, or AKAP350, is found at the MTOC in most cells but is not restricted to this location. 13,14 This molecule is a member of the AKAP (A-kinase anchoring proteins) family and recruits numerous proteins involved in signal transduction. In addition to protein kinases, such as PKA, protein kinase N, or protein kinase C-⑀ (PKC-⑀), AKAP450 also anchors phosphatases, including protein phosphatase 1 (PP1) and PP2A. 13,15,16 Specific displacement of endogenous AKAP450 by expression of the AKAP450 C-terminus, which contains the MTOC-targeting domain but not its coiled-coil domains or binding sites for signaling molecules, disrupts centrosomal function and induces cell-cycle arrest at G 1 in HeLa cells, showing defects in cytokinesis. 17 In addition, Ran-GTP, involved in nuclear import and export proteins and microtubule nucleation, associates with AKAP450 at the MTOC. 18 AKAP450 is also a component of the LFA-1-induced signaling complex involved in T-cell migration 19 ; integrins, particularly LFA-1, are critical for leukocyte migration and for the correct formation of the IS. 20 Furthermore, AKAP450 interacts with the dynein/dynactin complex, and this may be involved in the binding of the GA to the MTOC. ...

show abstract

“…Toca-1 is a member of the PCH (pombe Cdc15 homology) protein family involved in actin-based functions including cell adhesion, motility and vesicle trafficking [191][192][193]. Interestingly, CIP4/2, a member of PCH family, is reportedly involved in the process of GLUT4 translocation through interacting with TC10, and overexpression of mutant forms of CIP4/2 containing an N-terminal deletion or with diminished TC10 binding, prevents insulin-induced GLUT4 translocation.…”

Section: (3) Actin Remodeling At the Tgn Plays A Role In Regulatmentioning

confidence: 99%

Insulin Receptor Signals Regulating GLUT4 Translocation and Actin Dynamics

Kanzaki

2006

Endocr J

132

View full text Add to dashboard Cite

Abstract. In skeletal muscle and adipose tissue, insulin-stimulated glucose uptake is dependent upon translocation of the insulin-responsive glucose transporter GLUT4 from intracellular storage compartments to the plasma membrane. This insulin-induced redistribution of GLUT4 protein is achieved through a series of highly organized membrane trafficking events, orchestrated by insulin receptor signals. Recently, several key molecules linking insulin receptor signals and membrane trafficking have been identified, and emerging evidence supports the importance of subcellular compartmentalization of signaling components at the right time and in the right place. In addition, the translocation of GLUT4 in adipocytes requires insulin stimulation of dynamic actin remodeling at the inner surface of the plasma membrane (cortical actin) and in the perinuclear region. This results from at least two independent insulin receptor signals, one leading to the activation of phosphatidylinositol (PI) 3-kinase and the other to the activation of the Rho family small GTP-binding protein TC10. Thus, both spatial and temporal regulations of actin dynamics, both beneath the plasma membrane and around endomembranes, by insulin receptor signals are also involved in the process of GLUT4 translocation.

show abstract

AKAP350 Interaction with cdc42 Interacting Protein 4 at the Golgi Apparatus

Cited by 60 publications

References 57 publications

Setting the F-BAR: Functions and regulation of the F-BAR protein family

Setting the F-BAR: Functions and regulation of the F-BAR protein family

Integrin and CD3/TCR activation are regulated by the scaffold protein AKAP450

Insulin Receptor Signals Regulating GLUT4 Translocation and Actin Dynamics

Contact Info

Product

Resources

About