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[ subject:"Chemistry, Biochemistry." ]
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Regulation of cellular functions of ...
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University of Illinois at Chicago.
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Regulation of cellular functions of PDZ domains by membrane lipids.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Regulation of cellular functions of PDZ domains by membrane lipids./
作者:
Tun, Moe Phyu.
面頁冊數:
92 p.
附註:
Adviser: Wonhwa Cho.
Contained By:
Dissertation Abstracts International69-09B.
標題:
Chemistry, Biochemistry. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3327454
ISBN:
9780549798330
Regulation of cellular functions of PDZ domains by membrane lipids.
Tun, Moe Phyu.
Regulation of cellular functions of PDZ domains by membrane lipids.
- 92 p.
Adviser: Wonhwa Cho.
Thesis (Ph.D.)--University of Illinois at Chicago, 2008.
PDZ domains are small (∼90-amino acid) modular domains that act as scaffolding proteins, organizing the membrane receptors, cytoskeletons and other cytoplasmic proteins to form multiprotein complexes. Here, we show that PDZ domains not only bind to proteins but also to membrane lipids. Isolated PDZ domains from various proteins are quantitatively analyzed for their lipid binding properties using Surface Plasmon Resonance (SPR) analysis. 37 out of 94 tested PDZ domains bind to membrane lipids with submicromolar affinity. We also investigated the subcellular localizations of isolated PDZ domains to better understand how lipid binding modulates their cellular localization. Results indicate that lipid binding is common for PDZ domains and important for their cellular functions. The lipid binding sites of Zona occluden (ZO) proteins, each containing three PDZ domains, were characterized in detail. With biophysical and biochemical methods, we show that the peptide and lipid binding sites of ZO PDZ2 domains are partially overlapping and mutually exclusive. Although lipid binding does not seem to be necessary for the plasma membrane localization of the ZO proteins, phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P 2) binding regulates the recruitment of ZO-2 to nuclear speckles and nucleoli. This study presents evidence that the PDZ domains may play important physiological and functional roles by interacting with proteins as well as lipids.
ISBN: 9780549798330Subjects--Topical Terms:
1017722
Chemistry, Biochemistry.
Regulation of cellular functions of PDZ domains by membrane lipids.
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PDZ domains are small (∼90-amino acid) modular domains that act as scaffolding proteins, organizing the membrane receptors, cytoskeletons and other cytoplasmic proteins to form multiprotein complexes. Here, we show that PDZ domains not only bind to proteins but also to membrane lipids. Isolated PDZ domains from various proteins are quantitatively analyzed for their lipid binding properties using Surface Plasmon Resonance (SPR) analysis. 37 out of 94 tested PDZ domains bind to membrane lipids with submicromolar affinity. We also investigated the subcellular localizations of isolated PDZ domains to better understand how lipid binding modulates their cellular localization. Results indicate that lipid binding is common for PDZ domains and important for their cellular functions. The lipid binding sites of Zona occluden (ZO) proteins, each containing three PDZ domains, were characterized in detail. With biophysical and biochemical methods, we show that the peptide and lipid binding sites of ZO PDZ2 domains are partially overlapping and mutually exclusive. Although lipid binding does not seem to be necessary for the plasma membrane localization of the ZO proteins, phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P 2) binding regulates the recruitment of ZO-2 to nuclear speckles and nucleoli. This study presents evidence that the PDZ domains may play important physiological and functional roles by interacting with proteins as well as lipids.
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