Biology Reference
In-Depth Information
CHAPTER TWO
True Arrestins and Arrestin-Fold
Proteins: A Structure-Based
Appraisal
,†,‡
*
CEA, IRTSV, Laboratoire Biologie ` Grande Echelle, F-38054, Grenoble, France
†
,†,‡
, Gérard Klein
*
Laurence Aubry
*
INSERM, U1038, F-38054, Grenoble, France
‡
Universit´ Joseph Fourier, F-38000, Grenoble, France
Contents
1.
Introduction
22
2. True Arrestins: A Structure Adapted to Multiple Scaffolding
23
2.1 Function of arrestins
23
2.2 Crystal structure of arrestins
24
2.3 Binding sites for the endocytic machinery on arrestin
'
s C-terminal tail
26
2.4 Sites of posttranslational modifications
27
2.5 Binding sites for inositol phosphates
28
2.6 Conservation analysis of essential residues among visual and b-arrestins
30
3. Novel Arrestin-Related Proteins
30
3.1 Mammalian ARRDCs
30
3.2 ARTs in yeast and fungi
33
3.3 Amoebal ADCs
35
4. Other Arrestin-Fold Proteins
35
4.1 VPS26, a component of the retromer
35
4.2 DSCR3, a VPS26-related protein
39
4.3 RGP1, yet another arrestin-fold protein
40
5. Are Arrestins and Arrestin-Fold Proteins Related by a Shared Mechanism
for Their Function?
42
6. Conclusion and Perspectives
46
References
49
Abstract
Arrestin-clan proteins are folded alike, a feature responsible for their recent grouping in
a single clan. In human, it includes the well-characterized visual and b-arrestins, the
arrestin domain-containing proteins (ARRDCs), isoforms of the retromer subunit
VPS26, and DSCR3, a protein involved in Down syndrome. A new arrestin-fold-predicted
protein, RGP1, described here may join the clan. Unicellular organisms like the yeast Sac-
charomyces cerevisiae or the amoeba Dictyostelium discoideum harbor VPS26, DSCR3,
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