Calcium control of neurotransmitter release

TC Südhof - Cold Spring Harbor perspectives in biology, 2012 - cshperspectives.cshlp.org
Upon entering a presynaptic terminal, an action potential opens Ca2+ channels, and
transiently increases the local Ca2+ concentration at the presynaptic active zone. Ca2+ then …

Cell Wall Integrity Signaling in Saccharomyces cerevisiae

DE Levin - Microbiology and molecular biology reviews, 2005 - Am Soc Microbiol
The yeast cell wall is a highly dynamic structure that is responsible for protecting the cell
from rapid changes in external osmotic potential. The wall is also critical for cell expansion …

The physiological structure of human C-reactive protein and its complex with phosphocholine

D Thompson, MB Pepys, SP Wood - Structure, 1999 - cell.com
Background: Human C-reactive protein (CRP) is the classical acute phase reactant, the
circulating concentration of which rises rapidly and extensively in a cytokine-mediated …

The extended protein kinase C superfamily

H MELLOR, PJ PARKER - Biochemical Journal, 1998 - portlandpress.com
Members of the mammalian protein kinase C (PKC) superfamily play key regulatory roles in
a multitude of cellular processes, ranging from control of fundamental cell autonomous …

Synaptotagmin I functions as a calcium regulator of release probability

R Fernández-Chacón, A Königstorfer, SH Gerber… - Nature, 2001 - nature.com
In all synapses, Ca2+ triggers neurotransmitter release to initiate signal transmission. Ca2+
presumably acts by activating synaptic Ca2+ sensors, but the nature of these sensors …

Mechanism of calcium gating in small-conductance calcium-activated potassium channels

XM Xia, B Fakler, A Rivard, G Wayman, T Johnson-Pais… - Nature, 1998 - nature.com
The slow afterhyperpolarization that follows an action potential is generated by the activation
of small-conductance calcium-activated potassium channels (SK channels). The slow …

EF-hand calcium-binding proteins

A Lewit-Bentley, S Réty - Current opinion in structural biology, 2000 - Elsevier
The EF-hand motif is the most common calcium-binding motif found in proteins. Several high-
resolution structures containing different metal ions bound to EF-hand sites have given new …

Structure, function, and control of phosphoinositide-specific phospholipase C

MJ Rebecchi, SN Pentyala - Physiological reviews, 2000 - journals.physiology.org
Phosphoinositide-specific phospholipase C (PLC) subtypes β, γ, and δ comprise a related
group of multidomain phosphodiesterases that cleave the polar head groups from inositol …

The C2 domain calcium‐binding motif: structural and functional diversity

EA Nalefski, JJ Falke - Protein Science, 1996 - Wiley Online Library
The C2 domain is a Ca2+‐binding motif of approximately 130 residues in length originally
identified in the Ca2+‐dependent isoforms of protein kinase C. Single and multiple copies of …

C2-domains, structure and function of a universal Ca2+-binding domain

J Rizo, TC Sudhof - Journal of Biological Chemistry, 1998 - ASBMB
A vast amount of protein sequence data accumulated over recent years has revealed that
protein modules are widespread in nature. Many intracellular and extracellular proteins …