scholarly journals Reorientation of the first signal-anchor sequence during potassium channel biogenesis at the Sec61 complex

2013 ◽  
Vol 456 (2) ◽  
pp. 297-309 ◽  
Author(s):  
Helen R. Watson ◽  
Lydia Wunderley ◽  
Tereza Andreou ◽  
Jim Warwicker ◽  
Stephen High
Keyword(s):  
Membrane Proteins ◽  
Potassium Channel ◽  
Dynamic Environment ◽  
Signal Anchor ◽  
Transmembrane Regions ◽  
Anchor Sequence

The Sec61 translocon provides an unexpectedly flexible and dynamic environment within which transmembrane regions of nascent polypeptides can be completely reoriented during the biosynthesis of multiple-spanning membrane proteins.

scholarly journals The calmodulin-like proteins AtCML4 and AtCML5 are single-pass membrane proteins targeted to the endomembrane system by an N-terminal signal anchor sequence

2016 ◽  
Vol 67 (13) ◽  
pp. 3985-3996 ◽  
Author(s):  
Henning Ruge ◽  
Sandra Flosdorff ◽  
Ingo Ebersberger ◽  
Fatima Chigri ◽  
Ute C. Vothknecht
Keyword(s):  
Membrane Proteins ◽  
Endomembrane System ◽  
Single Pass ◽  
Signal Anchor ◽  
Anchor Sequence

scholarly journals Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence.

1993 ◽  
Vol 268 (34) ◽  
pp. 25265-25268 ◽  
Author(s):  
M Nguyen ◽  
D G Millar ◽  
V W Yong ◽  
S J Korsmeyer ◽  
G C Shore
Keyword(s):  
Outer Membrane ◽  
Mitochondrial Outer Membrane ◽  
Signal Anchor ◽  
Anchor Sequence

scholarly journals Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence

2017 ◽  
Vol 45 (20) ◽  
pp. 11858-11866 ◽  
Author(s):  
Evan Mercier ◽  
Wolf Holtkamp ◽  
Marina V. Rodnina ◽  
Wolfgang Wintermeyer
Keyword(s):  
Signal Recognition Particle ◽  
Signal Recognition ◽  
Signal Anchor ◽  
Anchor Sequence

scholarly journals Novel Molecular Biomarkers at the Blood-Brain Barrier in ALS

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Danijela Bataveljic ◽  
Milena Milosevic ◽  
Lidija Radenovic ◽  
Pavle Andjus
Keyword(s):  
Membrane Proteins ◽  
Potassium Channel ◽  
Blood Brain Barrier ◽  
Disease Onset ◽  
Water Channel ◽  
Aquaporin 4 ◽  
Brain Barrier ◽  
Inwardly Rectifying Potassium Channel ◽  
Blood Brain ◽  
Inwardly Rectifying

Recently neuroinflammation has gained a particular focus as a key mechanism of ALS. Several studiesin vivoas well asin vitrohave nominated immunoglobulin G (IgG) isolated from ALS patients as an active contributor to disease onset and progression. We have shown that ALS IgG affects astroglial Ca2+excitability and induces downstream activation of phosphatidylinositol 3-kinase. These studies were hampered by a lack of knowledge of the pathway of entry of immune factors in the CNS. Our MRI data revealed the blood-brain barrier BBB leakage and T cell infiltration into brain parenchyma in ALS G93A rats. Since astrocyte ensheathes blood vessel wall contributing to BBB stability and plays an important role in ALS pathogenesis, we have studied astrocytic membrane proteins water channel aquaporin-4 and the inwardly rectifying potassium channel. In this review, we will summarize data related to BBB disruption with particular emphasis on impaired function of astrocytes in ALS. We will discuss implication of membrane proteins expressed on astrocytic endfeet, aquaporin-4, and inwardly rectifying potassium channel in the pathology of ALS. In addition to ALS-specific IgGs, these membrane proteins are proposed as novel biomarkers of the disease.

scholarly journals Intramembrane Proteolysis and Endoplasmic Reticulum Retention of Hepatitis C Virus Core Protein

2004 ◽  
Vol 78 (12) ◽  
pp. 6370-6380 ◽  
Author(s):  
Kiyoko Okamoto ◽  
Kohji Moriishi ◽  
Tatsuo Miyamura ◽  
Yoshiharu Matsuura
Keyword(s):  
Endoplasmic Reticulum ◽  
Hepatitis C ◽  
Core Protein ◽  
Signal Sequence ◽  
Hydrophobic Region ◽  
E1 Protein ◽  
Hcv Core Protein ◽  
Er Retention ◽  
Signal Anchor ◽  
Anchor Sequence

ABSTRACT Hepatitis C virus (HCV) core protein is suggested to localize to the endoplasmic reticulum (ER) through a C-terminal hydrophobic region that acts as a membrane anchor for core protein and as a signal sequence for E1 protein. The signal sequence of core protein is further processed by signal peptide peptidase (SPP). We examined the regions of core protein responsible for ER retention and processing by SPP. Analysis of the intracellular localization of deletion mutants of HCV core protein revealed that not only the C-terminal signal-anchor sequence but also an upstream hydrophobic region from amino acid 128 to 151 is required for ER retention of core protein. Precise mutation analyses indicated that replacement of Leu139, Val140, and Leu144 of core protein by Ala inhibited processing by SPP, but cleavage at the core-E1 junction by signal peptidase was maintained. Additionally, the processed E1 protein was translocated into the ER and glycosylated with high-mannose oligosaccharides. Core protein derived from the mutants was translocated into the nucleus in spite of the presence of the unprocessed C-terminal signal-anchor sequence. Although the direct association of core protein with a wild-type SPP was not observed, expression of a loss-of-function SPP mutant inhibited cleavage of the signal sequence by SPP and coimmunoprecipitation with unprocessed core protein. These results indicate that Leu139, Val140, and Leu144 in core protein play crucial roles in the ER retention and SPP cleavage of HCV core protein.

Sign in / Sign up

Export Citation Format

Share Document