Study of desmin interactions with mitochondrial and lysosomal proteins

Postgraduate Thesis uoadl:1312444 268 Read counter

Unit:
Διατμηματικό / Διϊδρυτικό ΠΜΣ Μοριακή Ιατρική
Library of the School of Health Sciences
Deposit date:
2015-12-08
Year:
2015
Author:
Τσιλαφάκης Κωνσταντίνος
Supervisors info:
Σανούδου Δέσποινα, Μαυροειδής Εμμανουήλ, Κοσσίδα Σοφία
Original Title:
Μελέτη της αλληλεπίδρασης της δεσμίνης με μιτοχονδριακές και λυσοσωματικές πρωτεΐνες
Languages:
Greek
Translated title:
Study of desmin interactions with mitochondrial and lysosomal proteins
Summary:
Understanding the structure and function of intermediate filament (IF) is
necessary in order to explain, why more than 70 related IF genes have evolved
in vertebrates while maintaining such dramatically tissue specific expression.
Desmin is a member of the large multigene family of IF proteins and is
specifically expressed in myocytes. In an effort to elucidate its
muscle-specific behaviour, we have used a yeast two hybrid system in order to
identify desmin’s head binding partners. We describe for the first time a
mitochondrial and a lysosomal protein (NDUFS2 and saposin D respectively) as
direct desmin binding partners, which confirmed with GST-pull down assay. By
in silico analysis we have predicted desmin head domain 3D structure and we
observed that identical regions in NDUFS2 and saposin D are interacting with a
specific domain in the desmin head (Arg16 to Ser32).
Keywords:
Desmin, NDUFS2, SaposinD, Mitochondria, Lysosomes
Index:
Yes
Number of index pages:
8-11
Contains images:
Yes
Number of references:
87
Number of pages:
78
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