The Role of Tryptophan Residues in an Integral Membrane Protein:  Diacylglycerol Kinase†

Biochemistry ◽  
2003 ◽  
Vol 42 (37) ◽  
pp. 11065-11073 ◽  
Author(s):  
Elizabeth H. Clark ◽  
J. Malcolm East ◽  
Anthony G. Lee
Keyword(s):  
Membrane Protein ◽  
Diacylglycerol Kinase ◽  
Integral Membrane Protein ◽  
Tryptophan Residues

scholarly journals Golgi membrane protein Erd1 Is essential for recycling a subset of Golgi glycosyltransferases

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Richa Sardana ◽  
Carolyn M Highland ◽  
Beth E Straight ◽  
Christopher F Chavez ◽  
J Christopher Fromme ◽  
...  
Keyword(s):  
Steady State ◽  
Membrane Protein ◽  
Integral Membrane Protein ◽  
Protein Glycosylation ◽  
Sequential Process ◽  
Golgi Membrane ◽  
Present Evidence ◽  
Cytosolic Receptor

Protein glycosylation in the Golgi is a sequential process that requires proper distribution of transmembrane glycosyltransferase enzymes in the appropriate Golgi compartments. Some of the cytosolic machinery required for the steady-state localization of some Golgi enzymes are known but existing models do not explain how many of these enzymes are localized. Here, we uncover the role of an integral membrane protein in yeast, Erd1, as a key facilitator of Golgi glycosyltransferase recycling by directly interacting with both the Golgi enzymes and the cytosolic receptor, Vps74. Loss of Erd1 function results in mislocalization of Golgi enzymes to the vacuole/lysosome. We present evidence that Erd1 forms an integral part of the recycling machinery and ensures productive recycling of several early Golgi enzymes. Our work provides new insights on how the localization of Golgi glycosyltransferases is spatially and temporally regulated, and is finely tuned to the cues of Golgi maturation.

Reconstitutive Refolding of Diacylglycerol Kinase, an Integral Membrane Protein†

Biochemistry ◽  
1999 ◽  
Vol 38 (49) ◽  
pp. 16373-16382 ◽  
Author(s):  
Bonnie M. Gorzelle ◽  
Joanna K. Nagy ◽  
Kirill Oxenoid ◽  
Willis L. Lonzer ◽  
David S. Cafiso ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Diacylglycerol Kinase ◽  
Integral Membrane Protein

scholarly journals Functional assessment of SLC4A11, an integral membrane protein mutated in corneal dystrophies

2016 ◽  
Vol 311 (5) ◽  
pp. C735-C748 ◽  
Author(s):  
Sampath K. Loganathan ◽  
Hans-Peter Schneider ◽  
Patricio E. Morgan ◽  
Joachim W. Deitmer ◽  
Joseph R. Casey
Keyword(s):  
Membrane Protein ◽  
Mammalian Cells ◽  
Expression System ◽  
Integral Membrane Protein ◽  
Normal Function ◽  
Hek293 Cells ◽  
Cell Swelling ◽  
Xenopus Laevis Oocytes ◽  
Corneal Dystrophies

SLC4A11, a member of the SLC4 family of bicarbonate transporters, is a widely expressed integral membrane protein, abundant in kidney and cornea. Mutations of SLC4A11 cause some cases of the blinding corneal dystrophies, congenital hereditary endothelial dystrophy, and Fuchs endothelial corneal dystrophy. These diseases are marked by fluid accumulation in the corneal stroma, secondary to defective fluid reabsorption by the corneal endothelium. The role of SLC4A11 in these corneal dystrophies is not firmly established, as SLC4A11 function remains unclear. To clarify the normal function(s) of SLC4A11, we characterized the protein following expression in the simple, low-background expression system Xenopus laevis oocytes. Since plant and fungal SLC4A11 orthologs transport borate, we measured cell swelling associated with accumulation of solute borate. The plant water/borate transporter NIP5;1 manifested borate transport, whereas human SLC4A11 did not. SLC4A11 supported osmotically driven water accumulation that was electroneutral and Na+ independent. Studies in oocytes and HEK293 cells could not detect Na+-coupled HCO3− transport or Cl−/HCO3− exchange by SLC4A11. SLC4A11 mediated electroneutral NH3 transport in oocytes. Voltage-dependent OH− or H+ movement was not measurable in SLC4A11-expressing oocytes, but SLC4A11-expressing HEK293 cells manifested low-level cytosolic acidification at baseline. In mammalian cells, but not oocytes, OH−/H+ conductance may arise when SLC4A11 activates another protein or itself is activated by another protein. These data argue against a role of human SLC4A11 in bicarbonate or borate transport. This work provides additional support for water and ammonia transport by SLC4A11. When expressed in oocytes, SLC4A11 transported NH3, not NH3/H+.

How to Prepare Membrane Proteins for Solid-State NMR: A Case Study on the α-Helical Integral Membrane Protein Diacylglycerol Kinase from E. coli

ChemBioChem ◽  
2005 ◽  
Vol 6 (9) ◽  
pp. 1693-1700 ◽  
Author(s):  
Mark Lorch ◽  
Salem Faham ◽  
Christoph Kaiser ◽  
Ingrid Weber ◽  
A. James Mason ◽  
...  
Keyword(s):  
Solid State ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Solid State Nmr ◽  
Diacylglycerol Kinase ◽  
Integral Membrane Protein ◽  
E Coli

Total Chemical Synthesis of the Integral Membrane Protein Influenza A Virus M2:  Role of Its C-Terminal Domain in Tetramer Assembly†

Biochemistry ◽  
1999 ◽  
Vol 38 (37) ◽  
pp. 11905-11913 ◽  
Author(s):  
Gerd G. Kochendoerfer ◽  
David Salom ◽  
James D. Lear ◽  
Rosemarie Wilk-Orescan ◽  
Stephen B. H. Kent ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Chemical Synthesis ◽  
Influenza A Virus ◽  
Influenza A ◽  
Integral Membrane Protein ◽  
Terminal Domain

scholarly journals Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein

1997 ◽  
Vol 72 (6) ◽  
pp. 2688-2701 ◽  
Author(s):  
O. Vinogradova ◽  
P. Badola ◽  
L. Czerski ◽  
F.D. Sönnichsen ◽  
C.R. Sanders
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Diacylglycerol Kinase ◽  
Integral Membrane Protein ◽  
Solution Nmr ◽  
Nmr Methods ◽  
Kinase A

scholarly journals The role of protein purification in the structure determination of an integral membrane protein

1996 ◽  
Vol 52 (a1) ◽  
pp. C141-C141
Author(s):  
G. McDermott ◽  
S. M. Prince ◽  
M. Z. Papiz ◽  
A. M. Hawthornthwaite-Lawless ◽  
A. A. Freer ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Purification ◽  
Structure Determination ◽  
Integral Membrane Protein
Sign in / Sign up

Export Citation Format

Share Document