scholarly journals Identification of the Plasma Membrane Ca2+-ATPase and of Its Autoinhibitory Domain

1995 ◽  
Vol 108 (1) ◽  
pp. 105-113 ◽  
Author(s):  
F. Rasi-Caldogno ◽  
A. Carnelli ◽  
M. I. De Michelis
Keyword(s):  
Plasma Membrane ◽  
Autoinhibitory Domain

Single-Molecule Dynamics Reveal an Altered Conformation for the Autoinhibitory Domain of Plasma Membrane Ca2+-ATPase Bound to Oxidatively Modified Calmodulin†

Biochemistry ◽  
2004 ◽  
Vol 43 (40) ◽  
pp. 12937-12944 ◽  
Author(s):  
Kenneth D. Osborn ◽  
Ryan K. Bartlett ◽  
Abhijit Mandal ◽  
Asma Zaidi ◽  
Ramona J. Bieber Urbauer ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Single Molecule ◽  
Autoinhibitory Domain ◽  
Single Molecule Dynamics ◽  
Oxidatively Modified ◽  
Molecule Dynamics

Phospholamban is related to the autoinhibitory domain of the plasma membrane calcium-pumping ATPase

Biochemistry ◽  
1991 ◽  
Vol 30 (32) ◽  
pp. 7978-7983 ◽  
Author(s):  
Michele Chiesi ◽  
Thomas Vorherr ◽  
Rocco Falchetto ◽  
Chantal Waelchli ◽  
Ernesto Carafoli
Keyword(s):  
Plasma Membrane ◽  
Autoinhibitory Domain

scholarly journals Interchange of autoinhibitory domain conformations in plasma-membrane Ca2+-ATPase-calmodulin complexes

2008 ◽  
Vol 17 (3) ◽  
pp. 555-562 ◽  
Author(s):  
Abhijit Mandal ◽  
Mangala Roshan Liyanage ◽  
Asma Zaidi ◽  
Carey K. Johnson
Keyword(s):  
Plasma Membrane ◽  
Autoinhibitory Domain

scholarly journals Multiple regulatory sites in the C-terminal autoinhibitory domain of the plasma membrane H+-ATPase

1995 ◽  
Vol 8 (6) ◽  
pp. 959-962 ◽  
Author(s):  
Anne Olsson ◽  
Fredrik Johansson ◽  
Marianne Sommarin ◽  
Christer Larsson
Keyword(s):  
Plasma Membrane ◽  
Autoinhibitory Domain ◽  
Regulatory Sites

scholarly journals Functional consequences of relocating the C-terminal calmodulin-binding autoinhibitory domains of the plasma membrane Ca2+ pump near the N-terminus

1998 ◽  
Vol 331 (3) ◽  
pp. 763-766 ◽  
Author(s):  
Hugo P. ADAMO ◽  
Mirta E. GRIMALDI
Keyword(s):  
Plasma Membrane ◽  
Maximal Activity ◽  
Terminal Segment ◽  
Acceptor Site ◽  
Wild Type ◽  
Autoinhibitory Domain ◽  
Calmodulin Binding ◽  
N Terminus ◽  
Maximal Activation ◽  
Functional Consequences

A mutant of the plasma membrane Ca2+ pump (PMCA) called (nCI)hPMCA4b(ct120), in which the C-terminal regulatory segment including the calmodulin-binding autoinhibitory domains C and I had been relocated near the N-terminus, has been expressed in COS-1 cells. The measurements of Ca2+ transport in microsomal preparations showed that the rearranged enzyme was functional. The activity of the (nCI)hPMCA4b(ct120) mutant was compared with those of the wild-type hPMCA4b and the fully active calmodulin-insensitive mutant hPMCA4b(ct120). In the absence of calmodulin the activity of (nCI)hPMCA4b(ct120) was higher than that of hPMCA4b but only 45% of that of hPMCA4b(ct120). Mutant (nCI)hPMCA4b(ct120) exhibited an apparent affinity for Ca2+ similar to that of hPMCA4b, typical of the inhibited state of the enzyme. Calmodulin at concentrations that fully activated hPMCA4b increased the activity of (nCI)hPMCA4b(ct120) to 68% of that of hPMCA4b(ct120). The lower maximal activity of (nCI)hPMCA4b(ct120) was not due to a lower affinity for calmodulin because the concentration of calmodulin required for half-maximal activation of (nCI)hPMCA4b(ct120) was equal to that of the wild-type hPMCA4b. These results indicate that (1) the disturbance of the N-terminal region of the PMCA by the insertion of the C-terminal segment decreased the ability of the pump to transport Ca2+, and (2) the calmodulin-binding autoinhibitory domain was still able to access its acceptor site from the N-terminal end of the molecule. However, although the calmodulin-binding and inhibitory functions of the C-domain were fully preserved, the I domain at its new position seemed less effective at inhibiting the pump.

Heterogeneity of Size and Distribution of Intramembrane Particles in the Plasma Membrane of Yeast

1977 ◽  
Vol 35 ◽  
pp. 596-597
Author(s):  
E. Keyhani
Keyword(s):  
Plasma Membrane ◽  
Candida Utilis ◽  
Synthetic Medium ◽  
Freeze Fracture ◽  
Translational Diffusion ◽  
Yeast Cells ◽  
Distilled Water ◽  
Intramembrane Particles ◽  
The Matrix ◽  
Water Cell

The matrix of biological membranes consists of a lipid bilayer into which proteins or protein aggregates are intercalated. Freeze-fracture techni- ques permit these proteins, perhaps in association with lipids, to be visualized in the hydrophobic regions of the membrane. Thus, numerous intramembrane particles (IMP) have been found on the fracture faces of membranes from a wide variety of cells (1-3). A recognized property of IMP is their tendency to form aggregates in response to changes in experi- mental conditions (4,5), perhaps as a result of translational diffusion through the viscous plane of the membrane. The purpose of this communica- tion is to describe the distribution and size of IMP in the plasma membrane of yeast (Candida utilis).Yeast cells (ATCC 8205) were grown in synthetic medium (6), and then harvested after 16 hours of culture, and washed twice in distilled water. Cell pellets were suspended in growth medium supplemented with 30% glycerol and incubated for 30 minutes at 0°C, centrifuged, and prepared for freeze-fracture, as described earlier (2,3).

Organization of the Pellicle and the Muciferous Glands in Euglena Gracilis

1970 ◽  
Vol 28 ◽  
pp. 104-105
Author(s):  
Hilton H. Mollenhauer ◽  
W. Evans
Keyword(s):  
Plasma Membrane ◽  
Euglena Gracilis ◽  
Complex Forms ◽  
Secondary Periodicity

The pellicular structure of Euglena gracilis consists of a series of relatively rigid strips (Fig. 1) composed of ridges and grooves which are helically oriented along the cell and which fuse together into a common junction at either end of the cell. The strips are predominantly protein and consist in part of a series of fibers about 50 Å in diameter spaced about 85 Å apart and with a secondary periodicity of about 450 Å. Microtubules are also present below each strip (Fig. 1) and are often considered as part of the pellicular complex. In addition, there may be another fibrous component near the base of the pellicle which has not yet been very well defined.The pellicular complex lies underneath the plasma membrane and entirely within the cell (Fig. 1). Each strip of the complex forms an overlapping junction with the adjacent strip along one side of each groove (Fig. 1), in such a way that a certain amount of sideways movement is possible between one strip and the next.

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