β-Arrestin 2-Dependent Angiotensin II Type 1A Receptor-Mediated Pathway of Chemotaxis

Hunton, Dacia L.; Barnes, William G.; Kim, Jihee; Ren, Xiu-Rong; Violin, Jonathan D.; Reiter, Eric; Milligan, Graeme; Patel, Dhavalkumar D.; Lefkowitz, Robert J.

doi:10.1124/mol.104.006270

Cited by 113 publications

(137 citation statements)

References 59 publications

(64 reference statements)

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“…In some cases the same receptor apparently uses different internalization pathways under different circumstances Lee et al, 2000). Arrestin was found to be necessary for desensitization but not for the internalization of some receptors , and even the active receptor conformation recognized by G proteins and GRKs/arrestins was reported to be different in some cases Vilardaga et al, 2001;Whistler et al, 2002b;Kohout et al, 2004;Hunton et al, 2005;Ponimaskin et al, 2005). Thus, one is left wondering whether these data can be reconciled with the "central dogma" of GRK and arrestin function in GPCR regulation.…”

Section: Introductionmentioning

confidence: 83%

The structural basis of arrestin-mediated regulation of G-protein-coupled receptors

Gurevich

2006

Pharmacology & Therapeutics

406

446

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The 4 mammalian arrestins serve as almost universal regulators of the largest known family of signaling proteins, G-protein-coupled receptors (GPCRs). Arrestins terminate receptor interactions with G proteins, redirect the signaling to a variety of alternative pathways, and orchestrate receptor internalization and subsequent intracellular trafficking. The elucidation of the structural basis and fine molecular mechanisms of the arrestin-receptor interaction paved the way to the targeted manipulation of this interaction from both sides to produce very stable or extremely transient complexes that helped to understand the regulation of many biologically important processes initiated by active GPCRs. The elucidation of the structural basis of arrestin interactions with numerous nonreceptor-binding partners is long overdue. It will allow the construction of fully functional arrestins in which the ability to interact with individual partners is specifically disrupted or enhanced by targeted mutagenesis. These "custom-designed" arrestin mutants will be valuable tools in defining the role of various interactions in the intricate interplay of multiple signaling pathways in the living cell. The identification of arrestin-binding sites for various signaling molecules will also set the stage for designing molecular tools for therapeutic intervention that may prove useful in numerous disorders associated with congenital or acquired disregulation of GPCR signaling.

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Section: Introductionmentioning

confidence: 83%

The structural basis of arrestin-mediated regulation of G-protein-coupled receptors

Gurevich

2006

Pharmacology & Therapeutics

406

446

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“…Also, a role for β-arrestin 2 in Angiotensin II receptor type 1A (AT 1A R) -stimulated chemotaxis has been observed. 35 The use of small interfering RNA directed at β-arrestin 2 almost abolished AT 1A R-mediated chemotaxis.…”

Section: β-Arrestin In Cellular Movementmentioning

confidence: 99%

Emerging Roles of β-Arrestins

Buchanan

DuBois²

2006

Cell Cycle

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Arrestins were originally characterized as structural adaptor proteins which modulate the desensitization and trafficking of seven-membrane-spanning receptors. From these seminal observations a multitude of novel functions for this gene family have arisen. Here we review the recently identified roles for β-arrestin including its nuclear function and roles in development, cellular migration, and metastasis.

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“…β-arrestins translocate from the cytoplasm to the nucleus and associate with transcription cofactors such as p300 and cAMP-response element-binding protein (CREB) at the promoters of target genes to promote transcription (Kang et al, 2005). β-arrestins are also involved in the development (Chen et al, 2004;Wilbanks et al, 2004) and cellular movement (Ge et al, 2004;Hunton et al, 2005; This study aims to analyze the expression of β-arrestin 1 in gastric cardiac adenocarcinoma and its relationships with clinicopathologic characteristics and survival status, which might help to investigate the functions of β-arrestin 1 in the differentiation and metastasis progression of gastric cardiac adenocarcinoma.…”

Section: Introductionmentioning

confidence: 99%

Expression of β-arrestin 1 in Gastric Cardiac Adenocarcinoma and its Relation with Progression

Wang

Su²,

2012

Asian Pacific Journal of Cancer Prevention

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Objective: Arrestins act as mediators of G protein-coupled receptor (GPCR) desensitization and trafficking, also actin as a scaffold for many intracellular signaling network. The role that β-arrestin 1 plays in gastric cardiac adenocarcinoma (GCA) and its clinicopathologic significance are untouched. Methods: Fifty patients with gastric cardiac adenocarcinoma were retrospectively enrolled and β-arrestin 1 was detected using immunohistochemistry in tissue samples. Results: Nuclear expression of β-arrestin 1 was observed in 78% of GCA samples (39/50) and cytoplasmic expression in 70% (35/50). β-arrestin 1 could be found in both nucleus and cytoplasm of 54% GCA (27/50) or in either of them in 94% (47/50). β-arrestin 1 protein positivity in well/ moderately differentiated carcinomas was significantly higher than that in poorly differentiated carcinomas (P=0.005). We found increased expression of β-arrestin 1 in cytoplasm was correlated with lymph nodal metastasis (P=0.002) and pathological lymph nodal staging (P=0.030). We also found β-arrestin 1 to be over-expressed in glandular epithelia cells of mucinous adenocarcinoma, a tumour type associated with an adverse outcome of gastric cardiac adenocarcinoma (P=0.022). Conclusion: β-arrestin 1 is over-expressed in the nucleus and/or cytoplasm of gastric cardiac adenocarcinoma. However, β-arrestin 1 has no relationship with the prognosis of gastric cardiac adenocarcinoma (P>0.05). Our data imply that β-arrestin 1 in cytoplasm may be involved in differentiation and metastasis of gastric cardiac adenocarcinoma.

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β-Arrestin 2-Dependent Angiotensin II Type 1A Receptor-Mediated Pathway of Chemotaxis

Cited by 113 publications

References 59 publications

The structural basis of arrestin-mediated regulation of G-protein-coupled receptors

The structural basis of arrestin-mediated regulation of G-protein-coupled receptors

Emerging Roles of β-Arrestins

Expression of β-arrestin 1 in Gastric Cardiac Adenocarcinoma and its Relation with Progression

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