Chapter category: Cell Metabolism
A Mutational Approach to Elucidate Annexin V Function
Annexins: Molecular Structure to Cellular Function
Edited by: Barbara A. SeatonISBN: 1-57059-316-7
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Chapter authors:
Begoña Campos, Jorge M. Naciff and John R. Dedman
Annexins mediate the intracellular calcium (Ca2+) signal by binding phospholipids in a Ca2+–dependent manner. Members of this protein family have been found in different phyla, ranging from single cell organisms to mammalian cells. Annexins compose up to 2% of the total tissue protein. They have been found in diverse tissues; individual annexins have distinct distributions. Annexins do not contain the E–F hand Ca2+–binding motif as found in calmodulin, nor do they possess sequence similarity with other Ca2+ and phospholipid binding proteins, such as protein kinase C.1 Amino acid sequence comparison within the annexin family reveals a highly conserved core structure of four repeated domains, each approximately 70 amino acids in length, preceded by a highly variable amino terminal region (see also chapter 1). Calcium and phospholipid binding properties are retained by the four domain protein core.2 The amino terminus of each annexin is unique in composition and in length. Annexins I, II, III, IV, VII, VIII, X and XII contain phosphorylation sites for protein kinase C.3,4 Annexins I and II are major substrates, respectively, for EGF receptor and p60src tyrosine kinases.5,6 It has been proposed that the amino terminal determines specific function(s) of the annexins. This idea is supported by the fact that this region influences the Ca2+ requirement for phospholipid binding.7,8,9,10
Additional chapters from this book:
Nematode Annexins
Carl E. Creutz
A major challenge in the annexin field at present is to clearly define the physiological roles of these proteins. One of the most promising approaches to determine the functions of annexins wi...
Transgenic Mouse Models: Studying the Function of Annexin VI In Vivo
Ann–Marie Gunteski–Hamblin and John R. Dedman
Transgenic mouse models have become powerful tools to study the func–tion of specific proteins in vivo. Current technology allows for the targeted overexpression of a specific gene to a s...
Clinical Applications of Annexins
Jonathan F. Tait
The discovery of the annexin protein family has led to much basic research on the structures, biochemical properties, and possible functions of these proteins. Although the physiological funct...
Annexin V and Cell Surface–Expressed Phosphatidylserine: A Revealing Pas de Deux
Chris P.M. Reutelingsperger and Waander L. van Heerde
Annexin V acquired the green card for its membership of the annexin family in 1987 when its primary structure was reported for the first time.1 Before 1987 annexin V was investigate...
The Biology of Annexin I
A. Ahluwalia, J. C. Buckingham, J. D. Croxtall, R. J. Flower, N. J. Goulding and M. Perretti
This chapter specifically addresses work which relates to the biological role of annexin I (generally referred to in our publications as lipocortin1) and its link with the actions of ho...
Annexin XI: A Calcyclin–Associated Nuclear Protein
Hiroyoshi Hidaka and Naoto Mamiya
Annexin XI, a novel annexin, was found as a protein with an apparent molecular weight of 50 kDa that bound to calcyclin in a calcium dependent manner. Therefore it was first termed CAP–50...
Annexin/Protein Interactions: Clues for Function
Adrian Sheldon and James M. Chen
The physiological roles of many proteins are often dictated by interac–tion with other proteins, enzymes or other ligands. The identification of such interactions can thus help to elucida...
Ca2+–Independent Functions of Annexins
A. Louise Upton, Helena C. Edwards and Stephen E. Moss
The annexins and the E–F hand proteins are the two largest families of calcium–binding proteins. The two groups are distinguished not only by their numerical size, but also by the ex...
Annexin Binding to Lipid Assemblies
Paul Meers
Proteins that transiently and peripherally associate with biological mem–branes are emerging as a large and important group responsible for some of the basic functions of cells. It has be...
Annexin Functions in Phagocytic Leukocytes
Joel D. Ernst
By a variety of approaches, annexins have been discovered as abundant proteins in phagocytic leukocytes. No essential role for any of the annexins has been firmly established, but recent studi...
Annexins and Membrane Traffic
Volker Gerke
Intracellular membrane traffic and the direction of flow of macromol–ecules within eukaryotic cells has attracted cell biologists for a long time. The extensive research in this area has ...
A Mutational Approach to Elucidate Annexin V Function
Begoña Campos, Jorge M. Naciff and John R. Dedman
Annexins mediate the intracellular calcium (Ca2+) signal by binding phospholipids in a Ca2+–dependent manner. Members of this protein family have been found in diffe...
A Common Trimer of Annexin V as a Basic Unit in 2D and 3D Crystal Forms
Alain Brisson and Anita Lewit–Bentley
Annexins constitute a family of proteins which share the property of binding to lipid membranes in a calcium–dependent manner.1–5 The binding of annexins to phospholipid s...
Three Dimensional Structure of Annexin IV
R. Bryan Sutton and Stephen R. Sprang
In this chapter we explore the architecture of annexin IV as revealed by X–ray crystallography. As the structure of this protein was only recently determined in our laboratory, we shall f...
Annexin V Molecular Structure, Ligand Binding and Biological Function
Barbara A. Seaton
This chapter introduces the molecular features that give rise to com–mon annexin properties. The first section describes the three dimensional structure of annexin V, the "prototypical" a...
Annexin Gene Structure
Nicholas J. Nevid and Nelson D. Horseman
The annexins comprise a relatively large family of calcium- and phos-pholipid-binding proteins. There are at least 10 distinct annexins in vertebrates (annexins I-VIII, XI and XIII), and addit...
