Involvement of Golgin-160 in Cell Surface Transport of Renal ROMK Channel: Co-expression of Golgin-160 Increases ROMK Currents

Bundis, Florian; Neagoe, Ioana; Schwappach, Blanche; Steinmeyer, Klaus

doi:10.1159/000091454

Cited by 21 publications

(14 citation statements)

References 48 publications

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“…In the case of golgin-160, the N-terminus mediates Golgi localization (Hicks and Machamer, 2002) and golgin-160 interacts with the ␤1-adrenergic receptor, which depends on golgin-160 for efficient trafficking out of the Golgi . Golgin-160 also promotes surface expression of a subset of potassium channels and the targeting of a glucose transporter (Bundis et al, 2006;Williams et al, 2006). An important future direction is using gene replacement of mutated forms of the golgins after siRNA-mediated knockdown (Pu- thenveedu and Linstedt, 2004) to determine which of the known activities are functionally required for Golgi membrane motility in living cells.…”

Section: Discussionmentioning

confidence: 99%

A Primary Role for Golgi Positioning in Directed Secretion, Cell Polarity, and Wound Healing

Yadav

Puri

Linstedt

2009

MBoC

269

308

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Peri-centrosomal positioning of the mammalian Golgi apparatus is known to involve microtubule-based motility, but its importance for cellular physiology is a major unanswered question. Here, we identify golgin-160 and GMAP210 as proteins required for centripetal motility of Golgi membranes. In the absence of either golgin, peri-centrosomal positioning of the Golgi apparatus was disrupted while the cytoskeleton remained intact. Although secretion persisted with normal kinetics, it was evenly distributed in response to wounding rather than directed to the wound edge. Strikingly, these cells also completely failed to polarize. Further, directionally persistent cell migration was inhibited such that wound closure was impaired. These findings not only reveal novel roles for golgin-160 and GMAP210 in conferring membrane motility but also indicate that Golgi positioning has an active role in directed secretion, cell polarity, and wound healing.

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Section: Discussionmentioning

confidence: 99%

A Primary Role for Golgi Positioning in Directed Secretion, Cell Polarity, and Wound Healing

Yadav

Puri

Linstedt

2009

MBoC

269

308

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“…Recent studies also indicate a role of Golga3 in membrane traffick- ing. When expressed in Xenopus oocytes, Golga3 facilitates the transport of the renal inward rectifier potassium channel to the cell surface (39). Golga3 was shown to interact with PIST, a protein involved in vesicular trafficking (32).…”

Section: Discussionmentioning

confidence: 99%

Modulation of D-Serine Levels via Ubiquitin-dependent Proteasomal Degradation of Serine Racemase

Dumin

Bendikov

Foltyn

et al. 2006

Journal of Biological Chemistry

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Mammalian serine racemase is a brain-enriched enzyme that converts L-into D-serine in the nervous system. D-Serine is an endogenous co-agonist at the "glycine site" of N-methyl D-aspartate (NMDA) receptors that is required for the receptor/ channel opening. Factors regulating the synthesis of D-serine have implications for the NMDA receptor transmission, but little is known on the signals and events affecting serine racemase levels. We found that serine racemase interacts with the Golgin subfamily A member 3 (Golga3) protein in yeast two-hybrid screening. The interaction was confirmed in vitro with the recombinant proteins in co-transfected HEK293 cells and in vivo by co-immunoprecipitation studies from brain homogenates. Golga3 and serine racemase co-localized at the cytosol, perinuclear Golgi region, and neuronal and glial cell processes in primary cultures. Golga3 significantly increased serine racemase steady-state levels in co-transfected HEK293 cells and primary astrocyte cultures. This observation led us to investigate mechanisms regulating serine racemase levels. We found that serine racemase is degraded through the ubiquitin-proteasomal system in a Golga3-modulated manner. Golga3 decreased the ubiquitylation of serine racemase both in vitro and in vivo and significantly increased the protein half-life in pulse-chase experiments. Our results suggest that the ubiquitin system is a main regulator of serine racemase and D-serine levels. Modulation of serine racemase degradation, such as that promoted by Golga3, provides a new mechanism for regulating brain D-serine levels and NMDA receptor activity.2 type of glutamate receptors play key roles in excitatory synaptic transmission and are involved in many physiological processes including learning and memory (1). NMDA receptor activity is tightly regulated, as its overactivation contributes to pathologic conditions such as stroke and neurodegenerative diseases (2). An interesting feature of NMDA receptors is the requirement of simultaneous binding of two agonists for channel opening, i.e. the NMDA channel only operates when both a glutamate site and a coagonist site are occupied (1). It has been shown that binding of glycine to the co-agonist site is an obligatory requirement for NMDA receptor/channel operation (3, 4). Subsequent studies have shown that brain D-serine is an endogenous ligand of the glycine site of NMDA receptors (5-9).Regulation of NMDA receptor activity by the co-agonist D-serine plays critical roles. Removal of endogenous D-serine decreases NMDA receptor responses (8) and blocks NMDAdependent migration of immature granule cells in the cerebellum (9). D-Serine is the dominant endogenous co-agonist for NMDA neurotoxicity, as removal of D-serine abolishes NMDA receptor-elicited cell death in hippocampal slices (6). In the vertebrate retina, endogenous D-serine mediates the light-dependent increase in neuronal activity by activating NMDA receptors (10). Furthermore, endogenous D-serine is required for the long term potentiation of the synaptic t...

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“…However, the function of golgin-160 under normal (nonapoptotic) conditions remains unknown. In this regard, golgin-160 has recently been shown to be involved in the trafficking of the ROMK potassium channel (Bundis et al, 2006) and the ␤-1 adrenergic receptor (Hicks et al, 2006). Golgin-160 has also been observed to directly associate with PIST (also known as GOPC, CAL, and FIG) that seems to be required for the vesicular trafficking of a subset of plasma membrane proteins (Hicks and Machamer, 2005).…”

Section: Introductionmentioning

confidence: 99%

Golgin-160 Is Required for the Golgi Membrane Sorting of the Insulin-responsive Glucose Transporter GLUT4 in Adipocytes

Williams

Hicks

Machamer

et al. 2006

MBoC

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The peripheral Golgi protein golgin-160 is induced during 3T3L1 adipogenesis and is primarily localized to the Golgi cisternae distinct from the trans-Golgi network (TGN) in a general distribution similar to p115. Small interfering RNA (siRNA)-mediated reduction in golgin-160 protein resulted in an increase accumulation of the insulin-responsive amino peptidase (IRAP) and the insulin-regulated glucose transporter (GLUT4) at the plasma membrane concomitant with enhanced glucose uptake in the basal state. The redistribution of GLUT4 was rescued by expression of a siRNA-resistant golgin-160 cDNA. The basal state accumulation of plasma membrane GLUT4 occurred due to an increased rate of exocytosis without any significant effect on the rate of endocytosis. This GLUT4 trafficking to the plasma membrane in the absence of golgin-160 was independent of TGN/Golgi sorting, because it was no longer inhibited by the expression of a dominant-interfering Golgi-localized, ␥-ear-containing ARF-binding protein mutant and displayed reduced binding to the lectin wheat germ agglutinin. Moreover, expression of the amino terminal head domain (amino acids 1-393) had no significant effect on the distribution or insulin-regulated trafficking of GLUT4 or IRAP. In contrast, expression of carboxyl ␣ helical region (393-1498) inhibited insulin-stimulated GLUT4 and IRAP translocation, but it had no effect on the sorting of constitutive membrane trafficking proteins, the transferrin receptor, or vesicular stomatitis virus G protein.Together, these data demonstrate that golgin-160 plays an important role in directing insulin-regulated trafficking proteins toward the insulin-responsive compartment in adipocytes. INTRODUCTIONGLUT4 is the facilitative glucose transporter that is primarily expressed in insulin-responsive tissues (i.e., striated muscle and adipose) and is responsible for the clearance of circulating glucose in the postprandial state (Mueckler, 1994;. Under basal conditions, the majority of GLUT4 is sequestered in specialized GLUT4 insulin-responsive storage compartments (IRCs). In response to insulin, GLUT4 translocates from these intracellular compartments and is functionally incorporated into the plasma membrane, thereby enhancing glucose uptake (Chang et al., 2004;Watson and Pessin, 2006). Despite the established importance of GLUT4 translocation in the regulation of glucose homeostasis, details of how muscle and adipose tissues maintain an insulin-sensitive IRC remain unknown.In a current model for GLUT4 compartmentalization, the newly synthesized GLUT4 protein is sorted directly into intracellular IRC (Watson et al., 2004). This process is different from the trafficking of related proteins (e.g., GLUT1) and other constitutively trafficking proteins (vesicular stomatitis virus G protein; VSV-G) that traffic directly to the plasma membrane after biosynthesis. The important initial biosynthetic processing steps that establish an insulin-responsive pool of GLUT4 are thought to take place in the sorting compartments of the trans-Gol...

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Involvement of Golgin-160 in Cell Surface Transport of Renal ROMK Channel: Co-expression of Golgin-160 Increases ROMK Currents

Cited by 21 publications

References 48 publications

A Primary Role for Golgi Positioning in Directed Secretion, Cell Polarity, and Wound Healing

A Primary Role for Golgi Positioning in Directed Secretion, Cell Polarity, and Wound Healing

Modulation of D-Serine Levels via Ubiquitin-dependent Proteasomal Degradation of Serine Racemase

Golgin-160 Is Required for the Golgi Membrane Sorting of the Insulin-responsive Glucose Transporter GLUT4 in Adipocytes

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