نتایج جستجو برای: pdz domain

تعداد نتایج: 406848  

2015
Marina E. Ivanova Georgina C. Fletcher Nicola O’Reilly Andrew G. Purkiss Barry J. Thompson Neil Q. McDonald

Many components of epithelial polarity protein complexes possess PDZ domains that are required for protein interaction and recruitment to the apical plasma membrane. Apical localization of the Crumbs (Crb) transmembrane protein requires a PDZ-mediated interaction with Pals1 (protein-associated with Lin7, Stardust, MPP5), a member of the p55 family of membrane-associated guanylate kinases (MAGUK...

Journal: :Cell 1996
Declan A. Doyle Alice Lee John Lewis Eunjoon Kim Morgan Sheng Roderick MacKinnon

Modular PDZ domains, found in many cell junction-associated proteins, mediate the clustering of membrane ion channels by binding to their C-terminus. The X-ray crystallographic structures of the third PDZ domain from the synaptic protein PSD-95 in complex with and in the absence of its peptide ligand have been determined at 1.8 angstroms and 2.3 angstroms resolution, respectively. The structure...

Journal: :Protein and peptide letters 2009
Shilong Fan Yingang Feng Zhiyi Wei Bin Xia Weimin Gong

Synbindin is one component of Transport protein particle (TRAPP) complexes. In the hippocampal neurons, synbindin binds syndecan-2 by its atypical PDZ domain (APD) and may regulate the formation of dendritic spines. To investigate the interaction of synbindin and syndecan-2, we determined the solution structure of the synbindin APD by NMR. The structure of APD is different from the classical ca...

2014
Sarah V. Consonni Patricia M. Brouwer Eleonora S. van Slobbe Johannes L. Bos

PDZGEF is a guanine nucleotide exchange factor for the small G protein Rap. It was recently found that PDZGEF contributes to establishment of intestinal epithelial polarity downstream of the kinase Lkb1. By binding to phosphatidic acid enriched at the apical membrane, PDZGEF locally activates Rap2a resulting in induction of brush border formation via a pathway that includes the polarity players...

2012
Ren Sheng Yong Chen Heon Yung Gee Ewa Stec Heather R. Melowic Nichole R. Blatner Moe P. Tun Yonjung Kim Morten Källberg Takahiro K. Fujiwara Ji Hye Hong Kwang Pyo Kim Hui Lu Akihiro Kusumi Min Goo Lee Wonhwa Cho

Cholesterol is known to modulate the physical properties of cell membranes, but its direct involvement in cellular signaling has not been thoroughly investigated. Here we show that cholesterol specifically binds many PDZ domains found in scaffold proteins, including the N-terminal PDZ domain of NHERF1/EBP50. This modular domain has a cholesterol-binding site topologically distinct from its cano...

2013
Sabiha R. Gardezi Qi Li Elise F. Stanley

Calcium entry through CaV2.2 calcium channels clustered at the active zone (AZ) of the presynaptic nerve terminal gates synaptic vesicle (SV) fusion and the discharge of neurotransmitters, but the mechanism of channel scaffolding remains poorly understood. Recent studies have implicated the binding of a PDZ ligand domain (PDZ-LD) at the tip of the channel C terminal to a partner PDZ domain on R...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2002
Nati Hernando Nadine Déliot Serge M Gisler Eleanor Lederer Edward J Weinman Jürg Biber Heini Murer

Type IIa Na/P(i) cotransporters are expressed in renal proximal brush border and are the major determinants of inorganic phosphate (P(i)) reabsorption. Their carboxyl-terminal tail contains information for apical expression, and interacts by means of its three terminal amino acids with several PSD95/DglA/ZO-1-like domain (PDZ)-containing proteins. Two of these proteins, NaPi-Cap1 and Na/H excha...

2016
Hongyun Nie Yueyue Liu Xiaolei Yin Huiren Cao Yanfei Wang Wei Xiong Yushuang Lin Zhigang Xu

Protocadherin 15 (PCDH15) is a core component of hair cell tip-links and crucial for proper function of inner ear hair cells. Mutations of PCDH15 gene cause syndromic and nonsyndromic hearing loss. At present, the regulatory mechanisms responsible for the intracellular transportation of PCDH15 largely remain unknown. Here we show that PIST, a Golgi-associated, PDZ domain-containing protein, int...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2015
Anna K de Regt Tania A Baker Robert T Sauer

Escherichia coli senses envelope stress using a signaling cascade initiated when DegS cleaves a transmembrane inhibitor of a transcriptional activator for response genes. Each subunit of the DegS trimer contains a protease domain and a PDZ domain. During stress, unassembled outer-membrane proteins (OMPs) accumulate in the periplasm and their C-terminal peptides activate DegS by binding to its P...

Journal: :American journal of physiology. Cell physiology 2005
Ryan R McWilliams Sophia Y Breusegem Kelley F Brodsky Eunjoon Kim Moshe Levi R Brian Doctor

Proteins expressing postsynaptic density (PSD)-95/Drosophila disk large (Dlg)/zonula occludens-1 (ZO-1) (PDZ) domains are commonly involved in moderating receptor, channel, and transporter activities at the plasma membrane in a variety of cell types. At the apical membrane of renal proximal tubules (PT), the type IIa NaP(i) cotransporter (NaP(i)-IIa) binds specific PDZ domain proteins. Shank2E ...

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