scholarly journals The Plasma Membrane Ca2+Pump Isoform 4a Differs from Isoform 4b in the Mechanism of Calmodulin Binding and Activation Kinetics

2007 ◽  
Vol 282 (35) ◽  
pp. 25640-25648 ◽  
Author(s):  
Ariel J. Caride ◽  
Adelaida G. Filoteo ◽  
John T. Penniston ◽  
Emanuel E. Strehler
Keyword(s):  
Plasma Membrane ◽  
Activation Kinetics ◽  
Calmodulin Binding

scholarly journals The Calmodulin Binding Domain of the Plasma Membrane Ca2+ Pump Interacts Both with Calmodulin and with Another Part of the Pump

1989 ◽  
Vol 264 (21) ◽  
pp. 12313-12321 ◽  
Author(s):  
A Enyedi ◽  
T Vorherr ◽  
P James ◽  
D J McCormick ◽  
A G Filoteo ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Binding Domain ◽  
Calmodulin Binding

scholarly journals Functions for Cdc42p BEM Adaptors in Regulating a Differentiation-Type MAP Kinase Pathway

2019 ◽  
Author(s):  
Sukanya Basu ◽  
Beatriz González ◽  
Boyang Li ◽  
Garrett Kimble ◽  
Keith G. Kozminski ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Polarity ◽  
Rho Gtpase ◽  
Mapk Pathway ◽  
Mitogen Activated Protein Kinase ◽  
List Type ◽  
Activation Kinetics ◽  
Closed Conformation ◽  
Mapk Pathways ◽  
Effector Pathways

ABSTRACTRho GTPases regulate cell polarity and signal transduction pathways to control morphogenetic responses in different settings. In yeast, the Rho GTPase Cdc42p regulates cell polarity, and through the p21-activated kinase Ste20p, Cdc42p also regulates mitogen-activated protein kinase (MAPK) pathways (mating, filamentous growth or fMAPK, and HOG). Although much is known about how Cdc42p regulates cell polarity and the mating pathway, how Cdc42p regulates the fMAPK pathway is not clear. To address this question, Cdc42p-dependent MAPK pathways were compared in the filamentous (∑1278b) strain background. Each MAPK pathway showed a unique activation profile, with the fMAPK pathway exhibiting slow activation kinetics compared to the mating and HOG pathways. A previously characterized version of Cdc42p, Cdc42pE100A, that is specifically defective for fMAPK pathway signaling, was defective for interaction with Bem4p, the pathway-specific adaptor for the fMAPK pathway. Corresponding residues in Bem4p were identified that were required for interaction with Cdc42p and fMAPK pathway signaling. The polarity adaptor Bem1p also regulated the fMAPK pathway. In the fMAPK pathway, Bem1p recruited Ste20p to the plasma membrane, cycled between an open and closed conformation, and interacted with the GEF for Cdc42, Cdc24p. Bem1p also regulated effector pathways in different ways, behaving as a multi-functional adaptor in some pathways and an inert scaffold in others. Genetic suppression tests showed that Bem4p and Bem1p regulate the fMAPK pathway in an ordered sequence. Collectively, the study demonstrates unique and sequential functions for Rho GTPase adaptors in regulating MAPK pathways.HIGHLIGHTSComparing Cdc42p-dependent MAPK pathways showed that the fMAPK pathway had slow activation kinetics compared to the mating and HOG pathways.A collection of cdc42 alleles was tested for MAPK pathway functions. § Cdc42pE100A, previously characterized as being specifically defective for fMAPK signaling, showed reduced interaction with the fMAPK pathway adaptor Bem4p.§ Corresponding residues in Bem4p were identified that were required for interaction with Cdc42p and fMAPK signaling.The polarity adaptor Bem1p regulated the fMAPK pathway. § Bem1p regulated the fMAPK pathway by recruiting Ste20p to the plasma membrane, cycling between an open and closed conformation, and interacting with the Cdc42p GEF, Cdc24p.Different domains of Bem1p had different roles in regulating effector pathways. § Bem1p may function as a multi-functional adaptor in some pathways and an inert scaffold in others.Bem4p and Bem1p regulated the fMAPK pathway in an ordered sequence. § The data support a model where Bem4p recruits Cdc24p to GDP-Cdc42p, and Bem1p directs GTP-Cdc42p to Ste20p at the plasma membrane.§ The bud-site GTPase Rsr1p regulates Cdc24p in the fMAPK pathway but does not initiate signaling.

scholarly journals A 36 kDa monomeric protein and its complex with a 10 kDa protein both isolated from bovine aorta are calpactin-like proteins that differ in their Ca2+-dependent calmodulin-binding and actin-severing properties

1988 ◽  
Vol 251 (3) ◽  
pp. 777-785 ◽  
Author(s):  
F Martin ◽  
J Derancourt ◽  
J P Capony ◽  
A Watrin ◽  
J C Cavadore
Keyword(s):  
Plasma Membrane ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Protein Complex ◽  
Actin Filaments ◽  
Thin Filament ◽  
Partial Amino Acid Sequence ◽  
Calmodulin Binding

Interaction of plasma membrane with the cytoskeleton involves a large number of proteins, among them a 36 kDa protein that was found to be involved in the interaction with actin filaments. We have isolated a 36 kDa protein from bovine aorta as a monomer and in a complex with a 10 kDa protein. Partial amino acid sequence determinations show that the 36 kDa and 10 kDa proteins isolated from bovine aorta are analogous to or identical with corresponding proteins purified from bovine intestine already described by Kristensen, Saris, Hunter, Hicks, Noonan, Glenney & Tack [(1986) Biochemistry 25, 4497-4503]. We report here that the association of the 10 kDa protein with the 36 kDa protein confers specific calmodulin-binding and actin-severing properties on the complex that are not possessed by the 36 kDa monomer alone. These findings suggest that the protein complex could be involved in thin-filament-related structures or could modulate some Ca2+-regulated events mediated by calmodulin.

scholarly journals The Calmodulin-binding Site of Sphingosine Kinase and Its Role in Agonist-dependent Translocation of Sphingosine Kinase 1 to the Plasma Membrane

2006 ◽  
Vol 281 (17) ◽  
pp. 11693-11701 ◽  
Author(s):  
Catherine M. Sutherland ◽  
Paul A. B. Moretti ◽  
Niamh M. Hewitt ◽  
Christopher J. Bagley ◽  
Mathew A. Vadas ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Binding Site ◽  
Sphingosine Kinase ◽  
Sphingosine Kinase 1 ◽  
Calmodulin Binding

scholarly journals Activation Kinetics of RAF Protein in the Ternary Complex of RAF, RAS-GTP, and Kinase on the Plasma Membrane of Living Cells

2011 ◽  
Vol 286 (42) ◽  
pp. 36460-36468 ◽  
Author(s):  
Kayo Hibino ◽  
Tatsuo Shibata ◽  
Toshio Yanagida ◽  
Yasushi Sako
Keyword(s):  
Plasma Membrane ◽  
Ternary Complex ◽  
Living Cells ◽  
Activation Kinetics ◽  
Kinetics Of

Interaction of calmodulin with the calmodulin binding domain of the plasma membrane calcium pump

Biochemistry ◽  
1990 ◽  
Vol 29 (2) ◽  
pp. 355-365 ◽  
Author(s):  
Thomas Vorherr ◽  
Peter James ◽  
Joachim Krebs ◽  
Agnes Enyedi ◽  
Daniel J. McCormick ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Binding Domain ◽  
Calcium Pump ◽  
Calmodulin Binding ◽  
Plasma Membrane Calcium Pump

scholarly journals Protein Kinase C Phosphorylates Plasma Membrane Ca2+Pump Isoform 4a at Its Calmodulin Binding Domain

1999 ◽  
Vol 274 (1) ◽  
pp. 527-531 ◽  
Author(s):  
Anil K. Verma ◽  
Katalin Paszty ◽  
Adelaida G. Filoteo ◽  
John T. Penniston ◽  
Agnes Enyedi
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Domain ◽  
Calmodulin Binding ◽  
Kinase C

Kinetic Analysis of the Calmodulin-Binding Region of the Plasma Membrane Calcium Pump Isoform 4b†

Biochemistry ◽  
2005 ◽  
Vol 44 (6) ◽  
pp. 2009-2020 ◽  
Author(s):  
Alan R. Penheiter ◽  
Adelaida G. Filoteo ◽  
John T. Penniston ◽  
Ariel J. Caride
Keyword(s):  
Plasma Membrane ◽  
Kinetic Analysis ◽  
Calcium Pump ◽  
Binding Region ◽  
Calmodulin Binding ◽  
Plasma Membrane Calcium Pump
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