The Golgi-associated PDZ Domain Protein PIST/GOPC Stabilizes the β1-Adrenergic Receptor in Intracellular Compartments after Internalization

Koliwer, Judith; Park, Minjong; Bauch, Carola; Zastrow, Mark von; Kreienkamp, Hans‐Jürgen

doi:10.1074/jbc.m114.605725

Cited by 34 publications

(36 citation statements)

References 32 publications

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“…Additional proteins may participate in stabilizing GPCRs within the recycling apparatus or facilitating their movement through the ASRT complex. The Golgi-associated protein interacting specifically with Tc10 (also called PIST, GOPC, CAL, or FIG), for instance, stabilizes the β 1 AR with the TGN, leading to activation of the MAPK pathway [68]. This may be a more general theme of formation, dissolution, and hand-off of GPCRs harboring PDZ ligands as they traverse the endocytic machinery.…”

Section: Asrt-mediated Endosome-to-plasma Membrane Recyclingmentioning

confidence: 99%

GPCR Signaling and Trafficking: The Long and Short of It

Pavlos

Friedman

2017

Trends in Endocrinology & Metabolism

161

121

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Emerging findings disclose unexpected components of G protein-coupled receptor (GPCR) signaling and cell biology. Select GPCRs exhibit classical signaling that is restricted to cell membranes and newly described persistent signaling that depends on internalization of the GPCR bound to β-arrestins. Termination of non-canonical endosomal signaling requires intraluminal acidification and sophisticated protein trafficking machineries. Recent studies reveal the structural determinants of the trafficking chaperones. This review summarizes advances in GPCR signaling and trafficking with a focus on the parathyroid hormone receptor as prototype, and the actin-SNX27-retromer tubule complex, an endosomal sorting hub responsible for recycling and preservation of cell surface receptors. The findings are integrated into a model of PTHR trafficking with implications for signal transduction, bone growth, and mineral-ion metabolism.

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Section: Asrt-mediated Endosome-to-plasma Membrane Recyclingmentioning

confidence: 99%

GPCR Signaling and Trafficking: The Long and Short of It

Pavlos

Friedman

2017

Trends in Endocrinology & Metabolism

161

121

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“…CAL is selectively localized to the trans-Golgi network in neurons as well as other cell types and interacts with Rab6a, a small GTPase implicated in Golgi-related trafficking pathways (Bergbrede et al, 2009;Valente et al, 2010;Chen et al, 2012). CAL reduces plasma membrane expression and recycling of b 1 AR, and interferes with both b 1 AR-mediated ERK signaling and postendocytotic receptor degradation via the lysosome (He et al, 2004;Koliwer et al, 2015). CAL overexpression retains SSTR5 in the Golgi apparatus, thereby reducing SSTR5 cell surface expression (Wente et al, 2005;Bauch et al, 2014).…”

Section: Pdz Proteins That Regulate Golgi Traffickingmentioning

confidence: 99%

PDZ Protein Regulation of G Protein–Coupled Receptor Trafficking and Signaling Pathways

Dunn

Ferguson

2015

Mol Pharmacol

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G protein-coupled receptors (GPCRs) contribute to the regulation of every aspect of human physiology and are therapeutic targets for the treatment of numerous diseases. As a consequence, understanding the myriad of mechanisms controlling GPCR signaling and trafficking is essential for the development of new pharmacological strategies for the treatment of human pathologies. Of the many GPCR-interacting proteins, postsynaptic density protein of 95 kilodaltons, disc large, zona occludens-1 (PDZ) domain-containing proteins appear most abundant and have similarly been implicated in disease mechanisms. PDZ proteins play an important role in regulating receptor and channel protein localization within synapses and tight junctions and function to scaffold intracellular signaling protein complexes. In the current study, we review the known functional interactions between PDZ domain-containing proteins and GPCRs and provide insight into the potential mechanisms of action. These PDZ domain-containing proteins include the membraneassociated guanylate-like kinases [postsynaptic density protein of 95 kilodaltons; synapse-associated protein of 97 kilodaltons; postsynaptic density protein of 93 kilodaltons; synapse-associated protein of 102 kilodaltons; discs, large homolog 5; caspase activation and recruitment domain and membrane-associated guanylate-like kinase domain-containing protein 3; membrane protein, palmitoylated 3; calcium/calmodulin-dependent serine protein kinase; membrane-associated guanylate kinase protein (MAGI)-1, MAGI-2, and MAGI-3], Na 1 /H 1 exchanger regulatory factor proteins (NHERFs) (NHERF1, NHERF2, PDZ domaincontaining kidney protein 1, and PDZ domain-containing kidney protein 2), Golgi-associated PDZ proteins (Ga-binding protein interacting protein, C-terminus and CFTR-associated ligand), PDZ domain-containing guanine nucleotide exchange factors (GEFs) 1 and 2, regulator of G protein signaling (RGS)-homology-RhoGEFs (PDZ domain-containing RhoGEF and leukemia-associated RhoGEF), RGS3 and RGS12, spinophilin and neurabin-1, SRC homology 3 domain and multiple ankyrin repeat domain (Shank) proteins (Shank1, Shank2, and Shank3), partitioning defective proteins 3 and 6, multiple PDZ protein 1, Tamalin, neuronal nitric oxide synthase, syntrophins, protein interacting with protein kinase C a 1, syntenin-1, and sorting nexin 27.

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“…Among the positive clones that activate all the three reporter genes ( HIS3 , ADE2 , and l acZ ), several clones encode the PDZ-containing, Golgi-associated chaperone protein PIST. PIST has been shown to play important roles in regulating the membrane targeting of several transmembrane proteins such as frizzled, somatostatin receptor subtype 5 (SSTR5) and β 1-adrenergic receptor ( β 1AR) [30–32]. …”

Section: Resultsmentioning

confidence: 99%

“…PIST is a PDZ-containing, Golgi-associated chaperone protein, also named as FIG, GOPC, or CAL. PIST plays important roles in regulating the membrane targeting of transmembrane proteins [30–32]. Notably, PIST was shown to colocalize with the early endosome marker Rab5 and the TGN/endosome marker Rab14 [39].…”

Section: Discussionmentioning

confidence: 99%

Plasma Membrane Targeting of Protocadherin 15 Is Regulated by the Golgi-Associated Chaperone Protein PIST

et al. 2016

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Protocadherin 15 (PCDH15) is a core component of hair cell tip-links and crucial for proper function of inner ear hair cells. Mutations of PCDH15 gene cause syndromic and nonsyndromic hearing loss. At present, the regulatory mechanisms responsible for the intracellular transportation of PCDH15 largely remain unknown. Here we show that PIST, a Golgi-associated, PDZ domain-containing protein, interacts with PCDH15. The interaction is mediated by the PDZ domain of PIST and the C-terminal PDZ domain-binding interface (PBI) of PCDH15. Through this interaction, PIST retains PCDH15 in the trans-Golgi network (TGN) and reduces the membrane expression of PCDH15. We have previously showed that PIST regulates the membrane expression of another tip-link component, cadherin 23 (CDH23). Taken together, our finding suggests that PIST regulates the intracellular trafficking and membrane targeting of the tip-link proteins CDH23 and PCDH15.

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The Golgi-associated PDZ Domain Protein PIST/GOPC Stabilizes the β1-Adrenergic Receptor in Intracellular Compartments after Internalization

Cited by 34 publications

References 32 publications

GPCR Signaling and Trafficking: The Long and Short of It

GPCR Signaling and Trafficking: The Long and Short of It

PDZ Protein Regulation of G Protein–Coupled Receptor Trafficking and Signaling Pathways

Plasma Membrane Targeting of Protocadherin 15 Is Regulated by the Golgi-Associated Chaperone Protein PIST

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