Scarface, a secreted serine protease-like protein, regulates polarized localization of laminin A at the basement membrane of the Drosophila embryo

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Standard

Scarface, a secreted serine protease-like protein, regulates polarized localization of laminin A at the basement membrane of the Drosophila embryo. / Sorrosal, Georgina; Pérez, Lidia; Herranz, Héctor; Milán, Marco.

I: E M B O Reports, Bind 11, Nr. 5, 2010, s. 373-9.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Sorrosal, G, Pérez, L, Herranz, H & Milán, M 2010, 'Scarface, a secreted serine protease-like protein, regulates polarized localization of laminin A at the basement membrane of the Drosophila embryo', E M B O Reports, bind 11, nr. 5, s. 373-9. https://doi.org/10.1038/embor.2010.43

APA

Sorrosal, G., Pérez, L., Herranz, H., & Milán, M. (2010). Scarface, a secreted serine protease-like protein, regulates polarized localization of laminin A at the basement membrane of the Drosophila embryo. E M B O Reports, 11(5), 373-9. https://doi.org/10.1038/embor.2010.43

Vancouver

Sorrosal G, Pérez L, Herranz H, Milán M. Scarface, a secreted serine protease-like protein, regulates polarized localization of laminin A at the basement membrane of the Drosophila embryo. E M B O Reports. 2010;11(5):373-9. https://doi.org/10.1038/embor.2010.43

Author

Sorrosal, Georgina ; Pérez, Lidia ; Herranz, Héctor ; Milán, Marco. / Scarface, a secreted serine protease-like protein, regulates polarized localization of laminin A at the basement membrane of the Drosophila embryo. I: E M B O Reports. 2010 ; Bind 11, Nr. 5. s. 373-9.

Bibtex

@article{8337ae189fd246b1861c75e5ac557ca6,
title = "Scarface, a secreted serine protease-like protein, regulates polarized localization of laminin A at the basement membrane of the Drosophila embryo",
abstract = "Cell-matrix interactions brought about by the activity of integrins and laminins maintain the polarized architecture of epithelia and mediate morphogenetic interactions between apposing tissues. Although the polarized localization of laminins at the basement membrane is a crucial step in these processes, little is known about how this polarized distribution is achieved. Here, in Drosophila, we analyse the role of the secreted serine protease-like protein Scarface in germ-band retraction and dorsal closure-morphogenetic processes that rely on the activity of integrins and laminins. We present evidence that scarface is regulated by c-Jun amino-terminal kinase and that scarface mutant embryos show defects in these morphogenetic processes. Anomalous accumulation of laminin A on the apical surface of epithelial cells was observed in these embryos before a loss of epithelial polarity was induced. We propose that Scarface has a key role in regulating the polarized localization of laminin A in this developmental context.",
keywords = "Animals, Basement Membrane, Body Patterning, Cell Adhesion, Cell Polarity, Drosophila Proteins, Drosophila melanogaster, Embryo, Nonmammalian, JNK Mitogen-Activated Protein Kinases, Laminin, Pseudopodia, Serine Proteases",
author = "Georgina Sorrosal and Lidia P{\'e}rez and H{\'e}ctor Herranz and Marco Mil{\'a}n",
year = "2010",
doi = "10.1038/embor.2010.43",
language = "English",
volume = "11",
pages = "373--9",
journal = "E M B O Reports",
issn = "1469-221X",
publisher = "Wiley-Blackwell",
number = "5",

}

RIS

TY - JOUR

T1 - Scarface, a secreted serine protease-like protein, regulates polarized localization of laminin A at the basement membrane of the Drosophila embryo

AU - Sorrosal, Georgina

AU - Pérez, Lidia

AU - Herranz, Héctor

AU - Milán, Marco

PY - 2010

Y1 - 2010

N2 - Cell-matrix interactions brought about by the activity of integrins and laminins maintain the polarized architecture of epithelia and mediate morphogenetic interactions between apposing tissues. Although the polarized localization of laminins at the basement membrane is a crucial step in these processes, little is known about how this polarized distribution is achieved. Here, in Drosophila, we analyse the role of the secreted serine protease-like protein Scarface in germ-band retraction and dorsal closure-morphogenetic processes that rely on the activity of integrins and laminins. We present evidence that scarface is regulated by c-Jun amino-terminal kinase and that scarface mutant embryos show defects in these morphogenetic processes. Anomalous accumulation of laminin A on the apical surface of epithelial cells was observed in these embryos before a loss of epithelial polarity was induced. We propose that Scarface has a key role in regulating the polarized localization of laminin A in this developmental context.

AB - Cell-matrix interactions brought about by the activity of integrins and laminins maintain the polarized architecture of epithelia and mediate morphogenetic interactions between apposing tissues. Although the polarized localization of laminins at the basement membrane is a crucial step in these processes, little is known about how this polarized distribution is achieved. Here, in Drosophila, we analyse the role of the secreted serine protease-like protein Scarface in germ-band retraction and dorsal closure-morphogenetic processes that rely on the activity of integrins and laminins. We present evidence that scarface is regulated by c-Jun amino-terminal kinase and that scarface mutant embryos show defects in these morphogenetic processes. Anomalous accumulation of laminin A on the apical surface of epithelial cells was observed in these embryos before a loss of epithelial polarity was induced. We propose that Scarface has a key role in regulating the polarized localization of laminin A in this developmental context.

KW - Animals

KW - Basement Membrane

KW - Body Patterning

KW - Cell Adhesion

KW - Cell Polarity

KW - Drosophila Proteins

KW - Drosophila melanogaster

KW - Embryo, Nonmammalian

KW - JNK Mitogen-Activated Protein Kinases

KW - Laminin

KW - Pseudopodia

KW - Serine Proteases

U2 - 10.1038/embor.2010.43

DO - 10.1038/embor.2010.43

M3 - Journal article

C2 - 20379222

VL - 11

SP - 373

EP - 379

JO - E M B O Reports

JF - E M B O Reports

SN - 1469-221X

IS - 5

ER -

ID: 119179414