571 / 2019-04-02 20:08:26

On the way to elucidate functions of the γ-secretase complex in Arabidopsis thaliana

γ-secretase,presenilin,endocytosis,FLS2,BRI1

全体主题 > Cell Biology

Gamma-secretase complex have been very extensively investigated in animals, particularly in humans, due to participation in the regulation of the Notch signaling pathway and in the processing of amyloid precursor protein (APP). In most cells, the complex includes: presenilin (PS1 or PS2), nicastrin (NCT), APH-1 (anterior pharynx-defective 1) and PEN-2 (presenilin enhancer 2), each subunit with at least one transmembrane domain. None of known major substrates of the animal γ-secretase complex, has been identified in plants. In A. thaliana protoplasts, the existing data confirm localization of γ-secretase subunit homologs within endomembrane system. γ-secretase has been hypothetically considered as complex regulating vesicular transport.
Interactions during endocytosis between γ-secretase complex and chosen receptor proteins - FLS2 and BRI1 was examined. Also the capability of complex to taking activity towards animals receptors: hTFR and EGFR was analyzed. These proteins aren’t the direct substrates of the complex, but their correct endocytosis depends on PS1/PS2 activity. The use of dedicated antibodies directed against members of the complex, could lead to revealing the existing interaction within the complex and disclose new protein candidates interacting with γ-secretase complex.
This research is supported by the National Science Centre in Poland (2012/05/B/NZ3/01026) to PW and European Funds 'Knowledge Education Development' (POWR.03.02.00-00-I006/17).