Reference Report

Reference
Citation	Martin-Bermudo, M.D., Brown, N.H. (2000). The localized assembly of extracellular matrix integrin ligands requires cell-cell contact. J. Cell Sci. 113(21): 3715--3723. (Export to RIS)
FlyBase ID	FBrf0130272
Publication Type	Research paper
PubMed ID	11034900
PubMed Abstract	The assembly of an organism requires the interaction between different layers of cells, in many cases via an extracellular matrix. In the developing Drosophila larva, muscles attach in an integrin-dependent manner to the epidermis, via a specialized extracellular matrix called tendon matrix. Tiggrin, a tendon matrix integrin ligand, is primarily synthesized by cells distant to the muscle attachment sites, yet it accumulates specifically at these sites. Previous work has shown that the PS integrins are not required for tiggrin localization, suggesting that there is redundancy among tiggrin receptors. We have examined this by testing whether the PS2 integrin can recruit tiggrin to ectopic locations within the Drosophila embryo. We found that neither the wild type nor modified forms of the PS2 integrin, which have higher affinity for tiggrin, can recruit tiggrin to new cellular contexts. Next, we genetically manipulated the fate of the muscles and the epidermal muscle attachment cells, which demonstrated that muscles have the primary role in recruiting tiggrin to the tendon matrix and that cell-cell contact is necessary for this recruitment. Thus we propose that the inherent polarity of the muscle cells leads to a molecular specialization of their ends, and interactions between the ends produces an integrin-independent tiggrin receptor. Thus, interaction between cells generates an extracellular environment capable of nucleating extracellular matrix assembly.
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Language of Publication	English
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Publication Type	Journal
Abbreviation	J. Cell Sci.
Title	Journal of Cell Science
Publication Year	1966-
ISBN/ISSN	0021-9533
Data from Reference
Aberrations (1)
	Df(2R)en^E
Alleles (20)
	Avic\GFP^{S65T.I167T.Scer\UAS.T:Myr-Src64B} Ecol\lacZ^sr-B14.0 en^E if^B4 if^C.Scer\UAS if^{Scer\UAS.cMBa} if^{Δcyt.Scer\UAS} inv^E mbc^C1 Mef2^22-21 mys¹¹ mys^{CCβ.Scer\UAS.T:Rnor\CD2} mys^din.Scer\UAS rhea¹ Scer\GAL4^69B Scer\GAL4^how-24B Scer\GAL4^Kr.PM Scer\GAL4^twi.PG Tig^x twi¹
Constructs (8)
	P{CCβ} P{GAL4-Kr.C} P{GAL4-twi.G} P{UAS-if.c/g} P{UAS-if.C} P{UAS-if.Δcyt} P{UAS-mys.din} P{UAS-Src-GFP(S65T/I167T)}
Genes (15)
	Avic\GFP Ecol\lacZ en if inv mbc Mef2 Mhc mys rhea Scer\GAL4 T:Myr-Src64B T:Rnor\CD2 Tig twi
Insertions (3)
	P{GawB}69B P{GawB}how^24B P{lwB}sr^B14.0