scholarly journals The Golgi Localization of GnTI Requires a Polar Amino Acid Residue within Its Transmembrane Domain

2019 ◽  
Vol 180 (2) ◽  
pp. 859-873 ◽  
Author(s):  
Jennifer Schoberer ◽  
Eva Liebminger ◽  
Ulrike Vavra ◽  
Christiane Veit ◽  
Clemens Grünwald-Gruber ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Transmembrane Domain ◽  
Polar Amino Acid ◽  
Golgi Localization

Transmembrane domain length determines intracellular membrane compartment localization of syntaxins 3, 4, and 5

2001 ◽  
Vol 281 (1) ◽  
pp. C215-C223 ◽  
Author(s):  
Robert T. Watson ◽  
Jeffrey E. Pessin
Keyword(s):  
Amino Acids ◽  
Plasma Membrane ◽  
Amino Acid ◽  
Glucose Transporter ◽  
Transmembrane Domain ◽  
Transmembrane Domains ◽  
Snare Protein ◽  
Glut 4 ◽  
Golgi Localization ◽  
Syntaxin 3

Insulin recruits glucose transporter 4 (GLUT-4) vesicles from intracellular stores to the plasma membrane in muscle and adipose tissue by specific interactions between the vesicle membrane-soluble N-ethylmaleimide-sensitive factor attachment protein target receptor (SNARE) protein VAMP-2 and the target membrane SNARE protein syntaxin 4. Although GLUT-4 vesicle trafficking has been intensely studied, few have focused on the mechanism by which the SNAREs themselves localize to specific membrane compartments. We therefore set out to identify the molecular determinants for localizing several syntaxin isoforms, including syntaxins 3, 4, and 5, to their respective intracellular compartments (plasma membrane for syntaxins 3 and 4; cis-Golgi for syntaxin 5). Analysis of a series of deletion and chimeric syntaxin constructs revealed that the 17-amino acid transmembrane domain of syntaxin 5 was sufficient to direct the cis-Golgi localization of several heterologous reporter constructs. In contrast, the longer 25-amino acid transmembrane domain of syntaxin 3 was sufficient to localize reporter constructs to the plasma membrane. Furthermore, truncation of the syntaxin 3 transmembrane domain to 17 amino acids resulted in a complete conversion to cis-Golgi compartmentalization that was indistinguishable from syntaxin 5. These data support a model wherein short transmembrane domains (≤17 amino acids) direct the cis-Golgi localization of syntaxins, whereas long transmembrane domains (≥23 amino acids) direct plasma membrane localization.

scholarly journals Characterization of the Golgi Retention Motif of Rift Valley Fever Virus GN Glycoprotein

2002 ◽  
Vol 76 (23) ◽  
pp. 12200-12210 ◽  
Author(s):  
Sonja R. Gerrard ◽  
Stuart T. Nichol
Keyword(s):  
Amino Acid ◽  
Golgi Apparatus ◽  
Rift Valley ◽  
Rift Valley Fever ◽  
Transmembrane Domain ◽  
Expression System ◽  
Valley Fever ◽  
Golgi Localization ◽  
The Family ◽  
Localization Signal

ABSTRACT As Rift Valley fever (RVF) virus, and probably all members of the family Bunyaviridae, matures in the Golgi apparatus, the targeting of the virus glycoproteins to the Golgi apparatus plays a pivotal role in the virus replication cycle. No consensus Golgi localization motif appears to be shared among the glycoproteins of these viruses. The viruses of the family Bunyaviridae synthesize their glycoproteins, GN and GC, as a polyprotein. The Golgi localization signal of RVF virus has been shown to reside within the GN protein by use of a plasmid-based transient expression system to synthesize individual GN and GC proteins. While the distribution of individually expressed GN significantly overlaps with cellular Golgi proteins such as β-COP and GS-28, GC expressed in the absence of GN localizes to the endoplasmic reticulum. Further analysis of expressed GN truncated proteins and green fluorescent protein/GN chimeric proteins demonstrated that the RVF virus Golgi localization signal mapped to a 48-amino-acid region of GN encompassing the 20-amino-acid transmembrane domain and the adjacent 28 amino acids of the cytosolic tail.

scholarly journals Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.

1987 ◽  
Vol 262 (8) ◽  
pp. 3754-3761
Author(s):  
A.J. Ganzhorn ◽  
D.W. Green ◽  
A.D. Hershey ◽  
R.M. Gould ◽  
B.V. Plapp
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Amino Acid Residue ◽  
Kinetic Characterization ◽  
Alcohol Dehydrogenases

scholarly journals Amino Acid Residue at the 165th Position Tunes Eyfp Chromophore Maturation. A Structure-Based Design

2021 ◽  
Author(s):  
Nadya V. Pletneva ◽  
Eugene G. Maksimov ◽  
Elena A. Protasova ◽  
Anastasia V. Mamontova ◽  
Tatiana R. Simonyan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue
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