A chymotrypsin-like serine protease interacts with the chitin synthase from the midgut of the tobacco hornworm
Autor(en): | Broehan, Gunnar Zimoch, Lars Wessels, Anton Ertas, Beyhan Merzendorfer, Hans |
Stichwörter: | Biology; chitin; chitin synthase; chymotrypsin-like protease; GENES; Life Sciences & Biomedicine - Other Topics; Manduca sexta; MANDUCA-SEXTA; MECHANISM; MEMBRANE; midgut; PERITROPHIC MATRIX; PURIFICATION; SACCHAROMYCES-CEREVISIAE; SYNTHETASE; V-ATPASE; YEAST | Erscheinungsdatum: | 2007 | Herausgeber: | COMPANY OF BIOLOGISTS LTD | Journal: | JOURNAL OF EXPERIMENTAL BIOLOGY | Volumen: | 210 | Ausgabe: | 20 | Startseite: | 3636 | Seitenende: | 3643 | Zusammenfassung: | The chitin portion of the peritrophic matrix in the midgut of the tobacco hornworm, Manduca sexta, is produced by chitin synthase 2 (CHS2), a transmembrane family II glycosyltransferase, located at the apical tips of brush border microvilli. To look for proteins that potentially interact with CHS2, we performed yeast two-hybrid screening, identifying a novel chymotrypsin-like protease (CTLP1) that binds to the extracellular carboxyterminal domain of CHS2. The occurrence of this interaction in vivo is supported by co-localization and co-immunoprecipitation data. Based on our findings we propose that chitin synthesis is controlled by an intestinal proteolytic signalling cascade linking chitin synthase activity to the nutritional state of the larvae. |
ISSN: | 00220949 | DOI: | 10.1242/jeb.008334 |
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geprüft am 18.05.2024