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Strukturně funkční studie N-koncové domény MP endocytického proteinu SGIP1 / Structure-function study of N-terminal domain of protein SGIP1

The cells are communicating with each other using membrane-bound receptors. These receptors can recognize various ligands. Signalling via receptors allows the cell to control energy homeostasis, cell growth, differentiation, signalling and migration. Many of membrane-bound receptors are dynamically exchanged between plasma membrane and internal endosomal compartments by exo- and endocytosis. The most studied mechanism of endocytosis is clathrin-mediated endocytosis. There are many proteins involved in the sophisticated endocytic machinery. So called adaptor proteins allow and/or facilitate proper selection of cargo, which should be internalized. Some of them help to curve the membrane and form a vesicle, some of them may have opposite effect. "Src Homology 3-Domain Growth Factor Receptor-Bound 2-Like (Endophilin) Interacting Protein 1" (SGIP1) might fall in this category. This protein influences endocannabinoid signalling probably via its effect on cannabinoid receptors endocytosis. SGIP1 was recently identified as a gene involved in regulation of energy metabolism with overexpression leading to obesity. The aim of this work is structural and functional analysis of SGIP1 membrane phospholipid-binding domain (MP-domain). This domain shares no sequence homology with any of known proteins. In this...

Identiferoai:union.ndltd.org:nusl.cz/oai:invenio.nusl.cz:337357
Date January 2014
CreatorsDvořáková, Michaela
ContributorsKonvalinka, Jan, Vaněk, Ondřej
Source SetsCzech ETDs
LanguageCzech
Detected LanguageEnglish
Typeinfo:eu-repo/semantics/masterThesis
Rightsinfo:eu-repo/semantics/restrictedAccess

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