scholarly journals A Cell-Surface Membrane Protein Signature for Glioblastoma

Cell Systems ◽  
2017 ◽  
Vol 4 (5) ◽  
pp. 516-529.e7 ◽  
Author(s):  
Dhimankrishna Ghosh ◽  
Cory C. Funk ◽  
Juan Caballero ◽  
Nameeta Shah ◽  
Katherine Rouleau ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Cell Surface ◽  
Surface Membrane ◽  
Cell Surface Membrane ◽  
A Cell ◽  
Protein Signature

Cloned Cytotoxic and Non-Cytotoxic Lymphocytes in Mouse and Man: Their Reactivities and a Large Cell Surface Membrane Protein (LMP) Differentiation Marker System

1981 ◽  
Vol 54 (1) ◽  
pp. 5-26 ◽  
Author(s):  
Fritz H. Bach ◽  
Barbara J. Alter ◽  
Michael B. Widmer ◽  
Miriam Segall ◽  
Brian Dlinlap
Keyword(s):  
Membrane Protein ◽  
Cell Surface ◽  
Surface Membrane ◽  
Large Cell ◽  
Cytotoxic Lymphocytes ◽  
Marker System ◽  
Cell Surface Membrane ◽  
Differentiation Marker

scholarly journals Bioluminescence Assay for Detecting Cell Surface Membrane Protein Expression

2011 ◽  
Vol 9 (1) ◽  
pp. 31-39 ◽  
Author(s):  
Mieko Kato ◽  
Tomoki Chiba ◽  
Min Li ◽  
Yoshiro Hanyu
Keyword(s):  
Membrane Protein ◽  
Cell Surface ◽  
Protein Expression ◽  
Surface Membrane ◽  
Cell Surface Membrane ◽  
Membrane Protein Expression ◽  
Bioluminescence Assay

scholarly journals Kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane

2012 ◽  
Vol 23 (15) ◽  
pp. 2917-2929 ◽  
Author(s):  
Emily Deutsch ◽  
Aubrey V. Weigel ◽  
Elizabeth J. Akin ◽  
Phil Fox ◽  
Gentry Hansen ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Cell Surface ◽  
Ion Channel ◽  
Protein Trafficking ◽  
Hippocampal Neurons ◽  
Surface Membrane ◽  
Cell Types ◽  
Homogeneous Surface ◽  
Hek Cells ◽  
Membrane Protein Trafficking

Voltage-gated K+ (Kv) channels regulate membrane potential in many cell types. Although the channel surface density and location must be well controlled, little is known about Kv channel delivery and retrieval on the cell surface. The Kv2.1 channel localizes to micron-sized clusters in neurons and transfected human embryonic kidney (HEK) cells, where it is nonconducting. Because Kv2.1 is postulated to be involved in soluble N-ethylmaleimide–sensitive factor attachment protein receptor–mediated membrane fusion, we examined the hypothesis that these surface clusters are specialized platforms involved in membrane protein trafficking. Total internal reflection–based fluorescence recovery after photobleaching studies and quantum dot imaging of single Kv2.1 channels revealed that Kv2.1-containing vesicles deliver cargo at the Kv2.1 surface clusters in both transfected HEK cells and hippocampal neurons. More than 85% of cytoplasmic and recycling Kv2.1 channels was delivered to the cell surface at the cluster perimeter in both cell types. At least 85% of recycling Kv1.4, which, unlike Kv2.1, has a homogeneous surface distribution, is also delivered here. Actin depolymerization resulted in Kv2.1 exocytosis at cluster-free surface membrane. These results indicate that one nonconducting function of Kv2.1 is to form microdomains involved in membrane protein trafficking. This study is the first to identify stable cell surface platforms involved in ion channel trafficking.

Proteomic Analysis of Cell Surface Membrane Proteins in Leukemic Cells

2007 ◽  
pp. 135-146
Author(s):  
Robert S. Boyd ◽  
Martin J. S. Dyer ◽  
Kelvin Cain
Keyword(s):  
Membrane Proteins ◽  
Cell Surface ◽  
Proteomic Analysis ◽  
Surface Membrane ◽  
Leukemic Cells ◽  
Cell Surface Membrane
Sign in / Sign up

Export Citation Format

Share Document