The mechanism of evagination of imaginal discs of Drosophila melanogaster

Fristrom, Dianne; Fristrom, James W.

doi:10.1016/0012-1606(75)90127-x

Cited by 188 publications

(76 citation statements)

References 48 publications

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“…Very specific localization of both was observed at the basal cell layer interface during two separate stages of adhesion (6 -8 h after puparium formation (APF) and 34 -42 h APF) (Fig. 2, A and AЈ and D-EЈ), similar to what was previously seen for integrins (40,46). Localization of both O-glycans and Tiggrin was diffuse during stages of separation of the epithelial cell layers (18 -20 h APF) (Fig.…”

Section: Point Mutations That Disrupt Pgant3 Catalytic Activity Resulsupporting

confidence: 82%

“…Tiggrin and O-Glycans Are Specifically Localized during Pupal Wing Development-Pupal wing development undergoes a series of apposition, adhesion, expansion, and separation phases to ensure proper morphogenesis and establishment of cell contacts (46). To obtain insight into the role of O-glycans and Tiggrin in integrin-mediated cell adhesion in the wing, we examined pupal wings at multiple different developmental stages.…”

Section: Point Mutations That Disrupt Pgant3 Catalytic Activity Resulmentioning

confidence: 99%

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An O-Glycosyltransferase Promotes Cell Adhesion during Development by Influencing Secretion of an Extracellular Matrix Integrin Ligand

Zhang

Tran

Hagen

2010

Journal of Biological Chemistry

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Protein secretion and localization are crucial during eukaryotic development, establishing local cell environments as well as mediating cell interactions, signaling, and adhesion. In this study, we demonstrate that the glycosyltransferase, pgant3, specifically modulates integrin-mediated cell adhesion by influencing the secretion and localization of the integrin ligand, Tiggrin. We demonstrate that Tiggrin is normally O-glycosylated and localized to the basal matrix where the dorsal and ventral cell layers adhere in wild type Drosophila wings. In pgant3 mutants, Tiggrin is no longer O-glycosylated and fails to be properly secreted to this basal cell layer interface, resulting in disruption of integrin-mediated cell adhesion in the wing. pgant3-mediated effects are dependent on enzymatic activity, as mutations that form a stable protein yet abrogate O-glycosyltransferase activity result in Tiggrin accumulation within the dorsal and ventral cells comprising the wing. Our results provide the first in vivo evidence for the role of O-glycosylation in the secretion of specific extracellular matrix proteins, thus altering the composition of the cellular "microenvironment" and thereby modulating developmentally regulated cell adhesion events. As alterations in cell adhesion are a hallmark of cancer progression, this work provides insight into the long-standing association between aberrant O-glycosylation and tumorigenesis.

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Section: Point Mutations That Disrupt Pgant3 Catalytic Activity Resulsupporting

confidence: 82%

Section: Point Mutations That Disrupt Pgant3 Catalytic Activity Resulmentioning

confidence: 99%

An O-Glycosyltransferase Promotes Cell Adhesion during Development by Influencing Secretion of an Extracellular Matrix Integrin Ligand

Zhang

Tran

Hagen

2010

Journal of Biological Chemistry

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Section: Methodsmentioning

confidence: 99%

“…The CYFP-HA fragment (YFP aa 156 -239) for N-terminal fusions was amplified per PCR from pSPYCE(MR) (29) with the following primers: 5Ј-YFP_C156-HA (CGG AAT TCA TGG ACA AGC AGA AGA ACG GC) and 3Ј-YFP_C156-HA (GCT CTA GAA GCG TAA TCT GGA ACA TCG). The myc-NYFP fragment (YFP aa 1-173) for C-terminal fusions was amplified per PCR from pSPYNE173 (29) with the following primers: 5Ј-mycϩYFP_N173 (CGG AAT TCT ATG GAG CAA AAG TTG ATT TC) and 3Ј-mycϩYFP_N173 (GCT CTA GAC TAC TCG ATG TTG TGG CGG). The NYFP-myc fragment (YFP aa 1-173) for N-terminal fusions was amplified per PCR from pSPYNE(R)173 (29) with the following primers: 5Ј-YFP_N173ϩmyc (CGG AAT TCA TGG TGA GCA AGG GCG AGG AGC) and 3Ј-YFP_N173ϩmyc (GCT CTA GAA AGA TCC TCC TCA GAA ATC AAC).…”

Section: Methodsmentioning

confidence: 99%

“…The myc-NYFP fragment (YFP aa 1-173) for C-terminal fusions was amplified per PCR from pSPYNE173 (29) with the following primers: 5Ј-mycϩYFP_N173 (CGG AAT TCT ATG GAG CAA AAG TTG ATT TC) and 3Ј-mycϩYFP_N173 (GCT CTA GAC TAC TCG ATG TTG TGG CGG). The NYFP-myc fragment (YFP aa 1-173) for N-terminal fusions was amplified per PCR from pSPYNE(R)173 (29) with the following primers: 5Ј-YFP_N173ϩmyc (CGG AAT TCA TGG TGA GCA AGG GCG AGG AGC) and 3Ј-YFP_N173ϩmyc (GCT CTA GAA AGA TCC TCC TCA GAA ATC AAC). All PCR products were cloned into the MCS of the pUAST vector via EcoRI and XbaI.…”

Section: Methodsmentioning

confidence: 99%

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WAVE Forms Hetero- and Homo-oligomeric Complexes at Integrin Junctions in Drosophila Visualized by Bimolecular Fluorescence Complementation

Gohl

Banovic

Grevelhörster

et al. 2010

Journal of Biological Chemistry

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Dynamic actin polymerization drives a variety of morphogenetic events during metazoan development. Members of the WASP/WAVE protein family are central nucleation-promoting factors. They are embedded within regulatory networks of macromolecular complexes controlling Arp2/3-mediated actin nucleation in time and space. WAVE (Wiskott-Aldrich syndrome protein family verprolin-homologous protein) proteins are found in a conserved pentameric heterocomplex that contains Abi, Kette/Nap1, Sra-1/CYFIP, and HSPC300. Formation of the WAVE complex contributes to the localization, activity, and stability of the various WAVE proteins. Here, we established the Bimolecular Fluorescence Complementation (BiFC) technique in Drosophila to determine the subcellular localization of the WAVE complex in living flies. Using different split-YFP combinations, we are able to visualize the formation of the WAVE-Abi complex in vivo. We found that WAVE also forms dimers that are capable of forming higher order clusters with endogenous WAVE complex components. The N-terminal WAVE homology domain (WHD) of the WAVE protein mediates both WAVE-Abi and WAVE-WAVE interactions. Detailed localization analyses show that formation of WAVE complexes specifically takes place at basal cell compartments promoting actin polymerization. In the wing epithelium, hetero-and homooligomeric WAVE complexes co-localize with Integrin and Talin suggesting a role in integrin-mediated cell adhesion. RNAi mediated suppression of single components of the WAVE and the Arp2/3 complex in the wing further suggests that WAVE-dependent Arp2/3-mediated actin nucleation is important for the maintenance of stable integrin junctions.Many biological processes are controlled by networks of interacting proteins organized in macromolecular complexes. Members of the WASP/WAVE 2 protein family are found to be part of such macromolecular complexes coordinating Arp2/3-mediated actin polymerization in time and space (1). Purification of these multiprotein complexes and studies of the underlying protein interactions in vitro have led to significant advances in our understanding of how these molecular machines control actin nucleation. WAVE proteins are found in a pentameric heterocomplex that contains Abi, Kette/ Nap1, Sra-1/CYFIP, and HSPC300 (2). The interactions within the complex are mediated by direct protein-protein interactions (3-6). The central subunit of the WAVE complex represents the Abelson interactor Abi, which directly binds WAVE, HSPC300, and Kette/Nap1 through different domains. Sra-1 is a peripheral subunit recruited by Kette/ Nap1 and links the complex to Rac1 signaling. The WAVE complex is essential for the localization, activity, and stability of the various WAVE proteins (5, 7-11).However, purification and reconstitution experiments are based on the removal of the interacting proteins from their endogenous cellular context. To visualize WAVE complex formation in living flies we established the bimolecular fluorescence complementation (BiFC) technique in Drosophila. The Bi...

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IMP-L3, a 20-hydroxyecdysone-responsive gene encodes Drosophila lactate dehydrogenase: Structural characterization and developmental studies

Abu-Shumays

Fristrom

1997

Dev. Genet.

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The mechanism of evagination of imaginal discs of Drosophila melanogaster

Cited by 188 publications

References 48 publications

An O-Glycosyltransferase Promotes Cell Adhesion during Development by Influencing Secretion of an Extracellular Matrix Integrin Ligand

An O-Glycosyltransferase Promotes Cell Adhesion during Development by Influencing Secretion of an Extracellular Matrix Integrin Ligand

WAVE Forms Hetero- and Homo-oligomeric Complexes at Integrin Junctions in Drosophila Visualized by Bimolecular Fluorescence Complementation

IMP-L3, a 20-hydroxyecdysone-responsive gene encodes Drosophila lactate dehydrogenase: Structural characterization and developmental studies

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