scholarly journals Ion Channels in Arabidopsis Plasma Membrane : Transport Characteristics and Involvement in Light-Induced Voltage Changes

1992 ◽  
Vol 99 (1) ◽  
pp. 96-102 ◽  
Author(s):  
E. P. Spalding ◽  
C. L. Slayman ◽  
M. H. M. Goldsmith ◽  
D. Gradmann ◽  
A. Bertl
Keyword(s):  
Plasma Membrane ◽  
Ion Channels ◽  
Membrane Transport ◽  
Induced Voltage

N-terminal acetylation of annexin A2 is required for S100A10 binding

2012 ◽  
Vol 393 (10) ◽  
pp. 1141-1150 ◽  
Author(s):  
Ali Reza Nazmi ◽  
Gabriel Ozorowski ◽  
Milena Pejic ◽  
Julian P. Whitelegge ◽  
Volker Gerke ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Plasma Membrane ◽  
Ion Channels ◽  
Complex Formation ◽  
Membrane Transport ◽  
Annexin A2 ◽  
Binding Motif ◽  
Porcine Tissue ◽  
Membrane Cytoskeleton ◽  
Mammalian Protein

Abstract Annexin A2 (AnxA2), a Ca2+-regulated phospholipid binding protein involved in membrane-cytoskeleton contacts and membrane transport, exists in two physical states, as a monomer or in a heterotetrameric complex mediated by S100A10. Formation of the AnxA2-S100A10 complex is of crucial regulatory importance because only the complex is firmly anchored in the plasma membrane, where it functions in the plasma membrane targeting/recruitment of certain ion channels and receptors. The S100A10 binding motif is located in the first 12 residues of the AnxA2 N-terminal domain, but conflicting reports exist as to the importance of N-terminal AnxA2 acetylation with regard to S100A10 binding. We show here that AnxA2 is subject to N-terminal modification when expressed heterologously in Escherichia coli. Met1 is removed and Ser2 is acetylated, yielding the same modification as the authentic mammalian protein. Bacterially expressed and N-terminally acetylated AnxA2 binds S100A10 with an affinity comparable to AnxA2 from porcine tissue and is capable of forming the AnxA2-S100A10 heterotetramer. Complex formation is competitively inhibited by acetylated but not by non-acetylated peptides covering the N-terminal AnxA2 sequence. These results demonstrate that N-terminal acetylation of AnxA2 is required for S100A10 binding and that this common eukaryotic modification is also obtained upon expression in bacteria.

Pharmacology and Regulation of the Ion Channels of the Brown Adipocyte Plasma Membrane

1994 ◽  
pp. 103-108
Author(s):  
A. Koivisto ◽  
T. Ringer ◽  
U. Ruß ◽  
J. Nedergaard ◽  
D. Siemen
Keyword(s):  
Plasma Membrane ◽  
Ion Channels ◽  
Brown Adipocyte

Topology Inversion of CYP2D6 in the Endoplasmic Reticulum Is Not Required for Plasma Membrane Transport

1998 ◽  
Vol 53 (3) ◽  
pp. 408-414 ◽  
Author(s):  
Jacqueline Loeper ◽  
Annie Le Berre ◽  
Denis Pompon
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Membrane Transport

Ion Channels in the Plasma Membrane of Plant Cells

1992 ◽  
pp. 225-236
Author(s):  
B. R. Terry ◽  
S. D. Tyerman ◽  
G. P. Findlay
Keyword(s):  
Plasma Membrane ◽  
Ion Channels ◽  
Plant Cells

scholarly journals LDL Cholesterol Recycles to the Plasma Membrane via a Rab8a-Myosin5b-Actin-Dependent Membrane Transport Route

2013 ◽  
Vol 27 (3) ◽  
pp. 249-262 ◽  
Author(s):  
Kristiina Kanerva ◽  
Riikka-Liisa Uronen ◽  
Tomas Blom ◽  
Shiqian Li ◽  
Robert Bittman ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Transport ◽  
Ldl Cholesterol
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