Book contents
- Frontmatter
- Contents
- Preface
- CHAPTER ONE CELL LINEAGE VS. INTERCELLULAR SIGNALING
- CHAPTER TWO THE BRISTLE
- CHAPTER THREE BRISTLE PATTERNS
- CHAPTER FOUR ORIGIN AND GROWTH OF DISCS
- CHAPTER FIVE THE LEG DISC
- CHAPTER SIX THE WING DISC
- CHAPTER SEVEN THE EYE DISC
- CHAPTER EIGHT HOMEOSIS
- EPILOGUE
- APPENDIX ONE Glossary of Protein Domains
- APPENDIX TWO Inventory of Models, Mysteries, Devices, and Epiphanies
- APPENDIX THREE Genes That Can Alter Cell Fates Within the (5-Cell) Mechanosensory Bristle Organ
- APPENDIX FOUR Genes That Can Transform One Type of Bristle Into Another or Into a Different Type of Sense Organ
- APPENDIX FIVE Genes That Can Alter Bristle Number by Directly Affecting SOP Equivalence Groups or Inhibitory Fields
- APPENDIX SIX Signal Transduction Pathways: Hedgehog, Decapentaplegic, and Wingless
- APPENDIX SEVEN Commentaries on the Pithier Figures
- References
- Index
APPENDIX ONE - Glossary of Protein Domains
Published online by Cambridge University Press: 03 December 2009
- Frontmatter
- Contents
- Preface
- CHAPTER ONE CELL LINEAGE VS. INTERCELLULAR SIGNALING
- CHAPTER TWO THE BRISTLE
- CHAPTER THREE BRISTLE PATTERNS
- CHAPTER FOUR ORIGIN AND GROWTH OF DISCS
- CHAPTER FIVE THE LEG DISC
- CHAPTER SIX THE WING DISC
- CHAPTER SEVEN THE EYE DISC
- CHAPTER EIGHT HOMEOSIS
- EPILOGUE
- APPENDIX ONE Glossary of Protein Domains
- APPENDIX TWO Inventory of Models, Mysteries, Devices, and Epiphanies
- APPENDIX THREE Genes That Can Alter Cell Fates Within the (5-Cell) Mechanosensory Bristle Organ
- APPENDIX FOUR Genes That Can Transform One Type of Bristle Into Another or Into a Different Type of Sense Organ
- APPENDIX FIVE Genes That Can Alter Bristle Number by Directly Affecting SOP Equivalence Groups or Inhibitory Fields
- APPENDIX SIX Signal Transduction Pathways: Hedgehog, Decapentaplegic, and Wingless
- APPENDIX SEVEN Commentaries on the Pithier Figures
- References
- Index
Summary
All protein domains that were mentioned in the text or tables are inventoried below. For further information, consult PROSITE (www.expasy.ch/prosite) or the following reviews: domains in general, DNA-binding domains, scaffolding domains, extracellular domains, domain classification, domain evolution, protein-protein binding, protein-peptide binding, receptor-ligand binding, signal transduction, and an inventory of fly protein domains.
D. melanogaster proteins vary in size from 21 a.a. (L38, a ribosomal protein) to 5201 a.a. (Kakapo, a cytoskeletal component needed for intercellular adhesion). The domains listed below vary from 4 a.a. (WRPW) to ∼270 a.a. (PAS).
N.B.: Customarily, “domain” denotes a motif in proteins, while “box” refers to DNA. Thus, for example, the homeobox encodes the homeodomain. “Repeat” does not connote identity within a protein (e.g., only 6 of the 38 residues are invariant among Notch's 36 EGF-like repeats), nor does it imply interchangeability. For instance, the LIM domains of Lim3 can replace those of Apterous in wing development but not in the CNS. Likewise, Cactus's ankyrin repeats cannot functionally substitute for those of Notch. The specificity of repeats is epitomized by the “arm” domain:
Although individual repeats within a single protein are only about 30% identical, they are highly conserved during evolution. Thus, corresponding repeats of armadillo and β-catenin (which are direct homologs) are very similar (e.g., repeat 1 of armadillo is 90% identical to repeat 1 of β-catenin). […]
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- Imaginal DiscsThe Genetic and Cellular Logic of Pattern Formation, pp. 257 - 265Publisher: Cambridge University PressPrint publication year: 2002