The human serotonin1A receptor exhibits G-protein-dependent cell surface dynamics

2006 ◽  
Vol 24 (1) ◽  
pp. 25-31 ◽  
Author(s):  
Thomas J. Pucadyil ◽  
Amitabha Chattopadhyay
Keyword(s):  
Cell Surface ◽  
G Protein ◽  
Surface Dynamics ◽  
Serotonin1a Receptor ◽  
Dependent Cell

G-Protein-Dependent Cell Surface Dynamics of the Human Serotonin1AReceptor Tagged to Yellow Fluorescent Protein†

Biochemistry ◽  
2004 ◽  
Vol 43 (50) ◽  
pp. 15852-15862 ◽  
Author(s):  
Thomas J. Pucadyil ◽  
Shanti Kalipatnapu ◽  
Kaleeckal G. Harikumar ◽  
Nandini Rangaraj ◽  
Sadashiva S. Karnik ◽  
...  
Keyword(s):  
Cell Surface ◽  
G Protein ◽  
Fluorescent Protein ◽  
Yellow Fluorescent Protein ◽  
Surface Dynamics ◽  
Dependent Cell

scholarly journals Understudied G Protein-Coupled Receptors in the Kidney

Nephron ◽  
2021 ◽  
pp. 1-4
Author(s):  
Nathan A. Zaidman ◽  
Jennifer L. Pluznick
Keyword(s):  
Renal Function ◽  
Cell Surface ◽  
Gene Family ◽  
G Protein ◽  
External Environment ◽  
G Protein Coupled Receptors ◽  
Surface Proteins ◽  
Cell Surface Proteins ◽  
Large Subset ◽  
G Protein Coupled

G protein-coupled receptors (GPCRs) are cell surface proteins which play a key role in allowing cells, tissues, and organs to respond to changes in the external environment in order to maintain homeostasis. Despite the fact that GPCRs are known to play key roles in a variety of tissues, there are a large subset of GPCRs that remain poorly studied. In this minireview, we will summarize what is known regarding the “understudied” GPCRs with respect to renal function, and in so doing will highlight the promise represented by studying this gene family.

scholarly journals Vesicular Transport Is Not Required for the Cytoplasmic Pool of Cholera Toxin To Interact with the Stimulatory Alpha Subunit of the Heterotrimeric G Protein

2004 ◽  
Vol 72 (12) ◽  
pp. 6826-6835 ◽  
Author(s):  
Ken Teter ◽  
Michael G. Jobling ◽  
Randall K. Holmes
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Cholera Toxin ◽  
G Protein ◽  
Vesicular Transport ◽  
Cytotoxic Action ◽  
Anterograde Transport ◽  
Heterotrimeric G Protein ◽  
Α Subunit ◽  
Vesicular Traffic

ABSTRACT Cholera toxin (CT) moves from the cell surface to the endoplasmic reticulum (ER) by retrograde vesicular transport. The catalytic A1 polypeptide of CT (CTA1) then crosses the ER membrane, enters the cytosol, ADP-ribosylates the stimulatory α subunit of the heterotrimeric G protein (Gsα) at the cytoplasmic face of the plasma membrane, and activates adenylate cyclase. The cytosolic pool of CTA1 may reach the plasma membrane and its Gsα target by traveling on anterograde-directed transport vesicles. We examined this possibility with the use of a plasmid-based transfection system that directed newly synthesized CTA1 to either the ER lumen or the cytosol of CHO cells. Such a system allowed us to bypass the CT retrograde trafficking itinerary from the cell surface to the ER. Previous work has shown that the ER-localized pool of CTA1 is rapidly exported from the ER to the cytosol. Expression of CTA1 in either the ER or the cytosol led to the activation of Gsα, and Gsα activation was not inhibited in transfected cells exposed to drugs that inhibit vesicular traffic. Thus, anterograde transport from the ER to the plasma membrane is not required for the cytotoxic action of CTA1.

scholarly journals Pannexin1 and Pannexin3 Delivery, Cell Surface Dynamics, and Cytoskeletal Interactions

2010 ◽  
Vol 285 (12) ◽  
pp. 9147-9160 ◽  
Author(s):  
Ruchi Bhalla-Gehi ◽  
Silvia Penuela ◽  
Jared M. Churko ◽  
Qing Shao ◽  
Dale W. Laird
Keyword(s):  
Cell Surface ◽  
Surface Dynamics

Incorporation of a charged amino acid into the membrane-spanning domain blocks cell surface transport but not membrane anchoring of a viral glycoprotein

1985 ◽  
Vol 5 (6) ◽  
pp. 1442-1448
Author(s):  
G A Adams ◽  
J K Rose
Keyword(s):  
Amino Acid ◽  
Cell Surface ◽  
G Protein ◽  
Abnormal Behavior ◽  
Animal Cells ◽  
Viral Glycoprotein ◽  
Protein Levels ◽  
Membrane Spanning ◽  
Membrane Anchoring ◽  
Isoleucine Residue

The membrane-spanning domain of the vesicular stomatitis virus glycoprotein (G protein) consists of a continuous stretch of 20 uncharged and mostly hydrophobic amino acids. We examined the effects of two mutations which change the amino acid sequence in this domain. These mutations were generated by oligonucleotide-directed mutagenesis of a cDNA clone encoding the G protein, and the altered G proteins were then expressed in animal cells. Replacement of an isoleucine residue in the center of this domain with a strongly polar but uncharged amino acid (glutamine) had no effect on membrane anchoring or transport of the protein to the cell surface. Replacement of this same isoleucine residue with a charged amino acid (arginine) generated a G protein that still spanned intracellular membranes but was not transported efficiently to the cell surface. The protein accumulated in the Golgi region in about 50% of the cells, and about 20% of the cells had detectable protein levels in a punctate pattern on the cell surface. In the remaining cells the protein accumulated in a vesicular pattern throughout the cytoplasm. Models which might explain the abnormal behavior of this protein are discussed.

Intracellular transport of the glycoprotein of VSV is inhibited by CCCP at a late stage of post-translational processing

1989 ◽  
Vol 92 (4) ◽  
pp. 633-642
Author(s):  
J.K. Burkhardt ◽  
Y. Argon
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Surface ◽  
G Protein ◽  
Vesicular Stomatitis Virus ◽  
Late Stage ◽  
Intracellular Transport ◽  
Post Translational Modifications ◽  
Glycoprotein G ◽  
Golgi Compartment ◽  
Vesicular Stomatitis

The appearance of newly synthesized glycoprotein (G) of vesicular stomatitis virus at the surface of infected BHK cells is inhibited reversibly by treatment with carbonylcyanide m-chlorophenylhydrazone (CCCP). Under the conditions used, CCCP treatment depleted the cellular ATP levels by 40–60%, consistent with inhibition of transport at energy-requiring stages. The G protein that accumulates in cells treated with CCCP is heterogeneous. Most of it is larger than the newly synthesized G protein, is acylated with palmitic acid, and is resistant to endoglycosidase H (Endo H). Most of the arrested G protein is also sensitive to digestion with neuraminidase, indicating that it has undergone at least partial sialylation. A minority of G protein accumulates under these conditions in a less-mature form, suggesting its inability to reach the mid-Golgi compartment. The oligosaccharides of this G protein are Endo-H-sensitive and seem to be partly trimmed. Whereas sialylated G protein was arrested intracellularly, fucose-labelled G protein was able to complete its transport to the cell surface, indicating that a late CCCP-sensitive step separates sialylation from fucosylation. These post-translational modifications indicate that G protein can be transported as far as the trans-Golgi in the presence of CCCP and is not merely arrested in the endoplasmic reticulum.

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