Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/50824

TitleYeast Gup1(2) proteins are homologues of the Hedgehog Morphogens Acyltransferases HHAT(L): facts and implications
Author(s)Lucas, Cândida
Ferreira, Célia
Cazzanelli, Giulia
Franco-Duarte, Ricardo
Tulha, Joana
KeywordsYeast
GUP
HHAT
Morphogenesis
Hedgehog
Issue date2016
PublisherMDPI AG
JournalJournal of Developmental Biology
Abstract(s)In multiple tissues, the Hedgehog secreted morphogen activates in the receiving cells a pathway involved in cell fate, proliferation and differentiation in the receiving cells. This pathway is particularly important during embryogenesis. The protein HHAT (Hedgehog O-acyltransferase) modifies Hh morphogens prior to their secretion, while HHATL (Hh O-acyltransferase-like) negatively regulates the pathway. HHAT and HHATL are homologous to Saccharomyces cerevisiae Gup2 and Gup1, respectively. In yeast, Gup1 is associated with a high number and diversity of biological functions, namely polarity establishment, secretory/endocytic pathway functionality, vacuole morphology and wall and membrane composition, structure and maintenance. Phenotypes underlying death, morphogenesis and differentiation are also included. Paracrine signalling, like the one promoted by the Hh pathway, has not been shown to occur in microbial communities, despite the fact that large aggregates of cells like biofilms or colonies behave as proto-tissues. Instead, these have been suggested to sense the population density through the secretion of quorum-sensing chemicals. This review focuses on Gup1/HHATL and Gup2/HHAT proteins. We review the functions and physiology associated with these proteins in yeasts and higher eukaryotes. We suggest standardisation of the presently chaotic Gup-related nomenclature, which includes KIAA117, c3orf3, RASP, Skinny, Sightless and Central Missing, in order to avoid the disclosure of otherwise unnoticed information.
TypeArticle
URIhttp://hdl.handle.net/1822/50824
DOI10.3390/jdb4040033
ISSN2221-3759
Peer-Reviewedyes
AccessOpen access
Appears in Collections:DBio - Artigos/Papers

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