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Citation	Hopmann, R., Cooper, J.A., Miller, K.G. (1996). Actin organization, bristle morphology, and viability are affected by actin capping protein mutations in Drosophila. J. Cell Biol. 133(6): 1293--1305.
FlyBase ID	FBrf0088213
Type of publication	Research paper
Offprint Available	No
External Crossreferences
PubMed ID	8682865
PubMed Abstract	Regulation of actin filament length and orientation is important in many actin-based cellular processes. This regulation is postulated to occur through the action of actin-binding proteins. Many actin-binding proteins that modify actin in vitro have been identified, but in many cases, it is not known if this activity is physiologically relevant. Capping protein (CP) is an actin-binding protein that has been demonstrated to control filament length in vitro by binding to the barbed ends and preventing the addition or loss of actin monomers. To examine the in vivo role of CP, we have performed a molecular and genetic characterization of the beta subunit of capping protein from Drosophila melanogaster. We have identified mutations in the Drosophila beta subunit-these are the first CP mutations in a multicellular organism, and unlike CP mutations in yeast, they are lethal, causing death during the early larval stage. Adult files that are heterozygous for a pair of weak alleles have a defect in bristle morphology that is correlated to disorganized actin bundles in developing bristles. Our data demonstrate that CP has an essential function during development, and further suggest that CP is required to regulate actin assembly during the development of specialized structures that depend on actin for their morphology.
Biosis	99083974
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Language of publication	English
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Abbreviation	J. Cell Biol.
Title	Journal of Cell Biology
Authors
Volume range	1-
Year range	1966-
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Place of publication	New York
Language of publication	English
ISBN/ISSN	0021-9525
CODEN	JCLBA3
Data from Reference
Aberrations (2)
	Df(2L)ast2 Df(2L)dp-79b
Alleles (4)
	cpb^+t4.5 cpb^6.15 cpb^F19 y^+mDint2
Constructs (1)
	P{cpb^+t4.5}
Genes (2)
	cpb y