Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD- as well as NADPH-binding domains of glutathione reductase

NADPH oxidase cytochrome b558 consists of two subunits, gp91-phox and p22-phox, defects of which result in chronic granulomatous disease (CGD). The nature of the interaction between these subunits has yet to be determined. Absence of p22-phox in autosomal CGD patient-derived B-cell lines results in detectable levels of an incompletely glycosylated gp91-phox precursor. We have detected this same precursor species in four cell lines from patients with the X-linked form of the disease due to mutations in gp91-phox. Such mutations should delineate regions of gp91-phox important for its biosynthesis, including stable association with p22-phox. One mutation mapped to the putative FAD-binding domain, one mapped to a potential haem-binding domain, and two involved the region encoded by exon 3.

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Structure of the XPA DNA binding domain and RPA high-affinity DNA binding domains on a model NER substrate

Acta Crystallographica Section A Foundations and Advances ◽

10.1107/s0108767319098003 ◽

2019 ◽

Vol 75 (a1) ◽

pp. a203-a203

Author(s):

Walter J. Chazin ◽

Agnieszka M. Topolska-Woś ◽

Norie Sugitani ◽

John J. Cordoba ◽

Hyun Suk Kim ◽

...

Keyword(s):

Dna Binding ◽

Binding Domain ◽

Dna Binding Domain ◽

Dna Binding Domains ◽

High Affinity ◽

Binding Domains

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On Reflexive Binding in North Sami

Nordlyd ◽

10.7557/12.35 ◽

2004 ◽

Vol 31 (4) ◽

Author(s):

Hanna Outakoski

Keyword(s):

Binding Domain ◽

Local Domain ◽

Binding Theory ◽

Binding Domains ◽

Complement Clause ◽

The Subject

Principle A of the Binding Theory states that an anaphor must be A-bound in the local domain containing it, its governor and an accessible subject. However, if the anaphor is contained in an infinitival complement clause, it may, in North Sami, be bound either by the clause-mate subject or by the subject of the tensed clause. Thus, it appears that there is a larger binding domain for anaphors in addition to that determined by the condition A of standard binding theory. This domain can in some languages, as in North Sami, be defined by the notion of Tense whereas in other languages this need not be case, as in English. This supports the approach that the characterization of binding domains is parameterized and that languages pick different values of the parameter.

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Rapid Estrogen-Induced Phosphorylation of the SRC-3 Coactivator Occurs in an Extranuclear Complex Containing Estrogen Receptor

Molecular and Cellular Biology ◽

10.1128/mcb.25.18.8273-8284.2005 ◽

2005 ◽

Vol 25 (18) ◽

pp. 8273-8284 ◽

Cited By ~ 54

Author(s):

Fuzhong F. Zheng ◽

Ray-Chang Wu ◽

Carolyn L. Smith ◽

Bert W. O'Malley

Keyword(s):

Estrogen Receptor ◽

Ligand Binding ◽

Direct Interaction ◽

Activation Function ◽

Estrogen Receptor Α ◽

Binding Domain ◽

Phosphorylation Sites ◽

Binding Domains ◽

Nongenomic Action ◽

Binding Groove

ABSTRACT SRC-3/AIB1/ACTR/pCIP/RAC3/TRAM1 is a primary transcriptional coregulator for estrogen receptor (ER). Six SRC-3 phosphorylation sites have been identified, and these can be induced by steroids, cytokines, and growth factors, involving multiple kinase signaling pathways. Using phosphospecific antibodies for six phosphorylation sites, we investigated the mechanisms involved in estradiol (E2)-induced SRC-3 phosphorylation and found that this occurs only when either activated estrogen receptor α (ERα) or activated ERβ is present. Both the activation function 1 and the ligand binding domains of ERα are required for maximal induction. Mutations in the coactivator binding groove of the ERα ligand binding domain inhibit E2-stimulated SRC-3 phosphorylation, as do mutations in the nuclear receptor-interacting domain of SRC-3, suggesting that ERα must directly contact SRC-3 for this posttranslational modification to take place. A transcriptionally inactive ERα mutant which localizes to the cytoplasm supports E2-induced SRC-3 phosphorylation. Mutations of the ERα DNA binding domain did not block this rapid E2-dependent SRC-3 phosphorylation. Together these data demonstrate that E2-induced SRC-3 phosphorylation is dependent on a direct interaction between SRC-3 and ERα and can occur outside of the nucleus. Our results provide evidence for an early nongenomic action of ER on SRC-3 that supports the well-established downstream genomic roles of estrogen and coactivators.

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Nucleotide-binding domains of human cystic fibrosis transmembrane conductance regulator: detailed sequence analysis and three-dimensional modeling of the heterodimer

Cellular and Molecular Life Sciences ◽

10.1007/s00018-003-3386-z ◽

2004 ◽

Vol 61 (2) ◽

pp. 230-242 ◽

Cited By ~ 34

Author(s):

I. Callebaut ◽

R. Eudes ◽

J.-P. Mornon ◽

P. Lehn

Keyword(s):

Cystic Fibrosis ◽

Sequence Analysis ◽

Three Dimensional ◽

Nucleotide Binding ◽

Transmembrane Conductance Regulator ◽

Transmembrane Conductance ◽

Three Dimensional Modeling ◽

Binding Domains ◽

Dimensional Modeling ◽

Cystic Fibrosis Transmembrane

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GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration

Journal of Cell Science ◽

10.1242/jcs.115.7.1497 ◽

2002 ◽

Vol 115 (7) ◽

pp. 1497-1510 ◽

Cited By ~ 11

Author(s):

Ri-ichiroh Manabe ◽

Mykola Kovalenko ◽

Donna J. Webb ◽

Alan Rick Horwitz

Keyword(s):

Leading Edge ◽

Binding Domain ◽

Cell Periphery ◽

Molecular Signaling ◽

Cytoskeletal Organization ◽

Signaling Complex ◽

Binding Domains ◽

Arf Gtpases ◽

Cytoplasmic Structures ◽

Signaling Components

GIT1 is a multidomain protein that is thought to function as an integrator of signaling pathways controlling vesicle trafficking, adhesion and cytoskeletal organization. It regulates ARF GTPases and has binding domains for paxillin and PIX, which is a PAK-binding protein and an exchange factor for Rac. We show that GIT1 cycles between at least three distinct subcellular compartments, including adhesion-like structures, the leading edge and cytoplasmic complexes. The cytoplasmic structures, which also contain paxillin, PAK and PIX, do not detectably co-localize with endosomal Golgi or membrane markers, suggesting that they represent a novel supramolecular complex. The GIT1 cytoplasmic complexes are motile and tended to move toward the cell periphery where they joined existing adhesions. In retracting regions of the cells, the GIT1 complexes moved away from the disassembling adhesions toward the cell body. Using deletion mutants, we have identified domains that target GIT1 to each of the compartments. Localization to adhesions and the leading edge requires the paxillin-binding domain, which comprises the C-terminal 140 residues (cGIT1), whereas targeting to the cytoplasmic complexes requires the central region that contains ankyrin repeats and the PIX-binding domain. Expression of GIT1 or cGIT, but not nGIT1 in which the paxillin-binding domain is deleted, increases the rate of migration and the size and number of protrusions. The latter are inhibited when GIT1 is co-expressed with a kinase-dead PAK, suggesting that the GIT1 interaction with PAK is required for enhanced migration and protrusive activity. Furthermore,GIT1 targets constitutively activated PAK to adhesions and the leading edge via its interaction with paxillin. Since expression of cGIT targets endogenous GIT1 to the leading edge, it appears that the leading edge is the location of GIT1 responsible for these activities. Thus, GIT1 is a component of a motile,multimolecular complex that traffics a set of signaling components to specific locations in the cell where they regulate localized activities.

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