English Journal

Gamma interferon-induced guanylate binding protein 1 is a novel actin cytoskeleton remodeling factor.

Ostler N, Britzen-Laurent N, Liebl A, Naschberger E, Lochnit G, Ostler M, Forster F, Kunzelmann P, Ince S, Supper V, Praefcke GJ, Schubert DW, Stockinger H, Herrmann C, Stürzl M.Author information Division of Molecular and Experimental Surgery, University Medical Center Erlangen, Friedrich Alexander University of Erlangen-Nuremberg, Erlangen, Germany.AbstractGamma interferon (IFN-γ) regulates immune defenses against viruses, intracellular pathogens, and tumors by modulating cell proliferation, migration, invasion, and vesicle trafficking processes. The large GTPase guanylate binding protein 1 (GBP-1) is among the cellular proteins that is the most abundantly induced by IFN-γ and mediates its cell biologic effects. As yet, the molecular mechanisms of action of GBP-1 remain unknown. Applying an interaction proteomics approach, we identified actin as a strong and specific binding partner of GBP-1. Furthermore, GBP-1 colocalized with actin at the subcellular level and was both necessary and sufficient for the extensive remodeling of the fibrous actin structure observed in IFN-γ-exposed cells. These effects were dependent on the oligomerization and the GTPase activity of GBP-1. Purified GBP-1 and actin bound to each other, and this interaction was sufficient to impair the formation of actin filaments in vitro, as demonstrated by atomic force microscopy, dynamic light scattering, and fluorescence-monitored polymerization. Cosedimentation and band shift analyses demonstrated that GBP-1 binds robustly to globular actin and slightly to filamentous actin. This indicated that GBP-1 may induce actin remodeling via globular actin sequestering and/or filament capping. These results establish GBP-1 as a novel member within the family of actin-remodeling proteins specifically mediating IFN-γ-dependent defense strategies.
Molecular and cellular biology.Mol Cell Biol.2014 Jan;34(2):196-209. doi: 10.1128/MCB.00664-13. Epub 2013 Nov 4.
Gamma interferon (IFN-γ) regulates immune defenses against viruses, intracellular pathogens, and tumors by modulating cell proliferation, migration, invasion, and vesicle trafficking processes. The large GTPase guanylate binding protein 1 (GBP-1) is among the cellular proteins that is the most abun
PMID 24190970

Localization of aPKC Lambda/Iota and Its Interacting Protein, Lgl2, Is Significantly Associated with Lung Adenocarcinoma Progression.

Imamura N, Horikoshi Y, Matsuzaki T, Toriumi K, Kitatani K, Ogura G, Masuda R, Nakamura N, Takekoshi S, Iwazaki M.AbstractAtypical protein kinase C lambda/iota (aPKC λ/ι) is expressed in several human cancers; however, the correlation between aPKC λ/ι localization and cancer progression in human lung adenocarcinoma (LAC) remains to be clarified. We found that patients with a high level of aPKC λ/ι expression in LAC had significantly shorter overall survival than those with a low level of aPKC λ/ι expression. In addition, localization of aPKC λ/ι in the apical membrane or at the cell-cell contact was associated with both lymphatic invasion and metastasis. The intercellular adhesion molecule, E-cadherin, was decreased in LACs with highly expressed aPKC λ/ι at the invasion site of tumor cells. This result suggested that the expression levels of aPKC λ/ι and E-cadherin reflect the progression of LAC. On double-immunohistochemical analysis, aPKC λ/ι and Lgl2, a protein that interacts with aPKC λ/ι, were co-localized within LACs. Furthermore, we found that Lgl2 bound the aPKC λ/ι-Par6 complex in tumor tissue by immune-cosedimentation analysis. Apical membrane localization of Lgl2 was correlated with lymphatic invasion and lymph node metastasis. These results thus indicate that aPKC λ/ι expression is altered upon the progression of LAC. This is also the first evidence to show aPKC λ/ι overexpression in LAC and demonstrates that aPKC λ/ι localization at the apical membrane or cell-cell contact is associated with lymphatic invasion and metastasis of the tumor.
The Tokai journal of experimental and clinical medicine.Tokai J Exp Clin Med.2013 Dec 20;38(4):146-58.
Atypical protein kinase C lambda/iota (aPKC λ/ι) is expressed in several human cancers; however, the correlation between aPKC λ/ι localization and cancer progression in human lung adenocarcinoma (LAC) remains to be clarified. We found that patients with a high level of aPKC λ/ι expression in L
PMID 24318287

Structure, biochemical characterization and analysis of the pleomorphism of carboxylesterase Cest-2923 from Lactobacillus plantarum WCFS1.

Benavente R, Esteban-Torres M, Acebrón I, de Las Rivas B, Muñoz R, Alvarez Y, Mancheño JM.Author information Department of Crystallography and Structural Biology, Institute of Physical Chemistry Rocasolano, CSIC, Madrid, Spain.AbstractThe hydrolase fold is one of the most versatile structures in the protein realm according to the diversity of sequences adopting such a three-dimensional architecture. In the present study, we clarified the crystal structure of the carboxylesterase Cest-2923 from the lactic acid bacterium Lactobacillus plantarum WCFS1 refined to 2.1 Å resolution, determined its main biochemical characteristics and also carried out an analysis of its associative behaviour in solution. We found that the versatility of a canonical α/β hydrolase fold, the basic framework of the crystal structure of Cest-2923, also extends to its oligomeric behaviour in solution. Thus, we discovered that Cest-2923 exhibits a pH-dependent pleomorphic behaviour in solution involving monomers, canonical dimers and tetramers. Although, at neutral pH, the system is mainly shifted to dimeric species, under acidic conditions, tetrameric species predominate. Despite these tetramers resulting from the association of canonical dimers, as is commonly found in many other carboxylesterases from the hormone-sensitive lipase family, they can be defined as 'noncanonical' because they represent a different association mode. We identified this same type of tetramer in the closest relative of Cest-2923 that has been structurally characterized: the sugar hydrolase YeeB from Lactococcus lactis. The observed associative behaviour is consistent with the different crystallographic results for Cest-2923 from structural genomics consortia. Finally, the presence of sulfate or acetate molecules (depending on the crystal form analysed) in the close vicinity of the nucleophile Ser116 allows us to identify interactions with the putative oxyanion hole and deduce the existence of hydrolytic activity within Cest-2923 crystals.
The FEBS journal.FEBS J.2013 Dec;280(24):6658-71. doi: 10.1111/febs.12569. Epub 2013 Nov 4.
The hydrolase fold is one of the most versatile structures in the protein realm according to the diversity of sequences adopting such a three-dimensional architecture. In the present study, we clarified the crystal structure of the carboxylesterase Cest-2923 from the lactic acid bacterium Lactobacil
PMID 24127688

Japanese Journal

Isolation of Pollen-expressed Actin as a Candidate Protein Interacting with S-RNase in Prunus avium L.

松本大生,田尾龍太郎
Journal of the Japanese Society for Horticultural Science 81(1), 41-47, 2012
… Furthermore, filamentous actin (F-Act) cosedimentation assay and 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) crosslinking assay using rabbit actin demonstrated that reduced S-RNases interacted with both F-Act and globular actin (G-Act). …
NAID 130004510740

Tetrahymena Fimbrin Localized in the Division Furrow Bundles Actin Filaments in a Calcium-Independent Manner

Shirayama Shin,Numata Osamu
The journal of biochemistry 134(4), 591-598, 2003-10-01
… In an F-actin cosedimentation assay, Tetrahymena fimbrin bound to F-actin and bundled it in a Ca2+-independent manner, with a Kd of 0.3 μM and a stoichiometry at saturation of 1:1.4 (Tetrahymena fimbrin: actin). …
NAID 10012058584

The Effect of Single Residue Substitutions of Serine-283 on the Strength of Head-to-Tail Interaction and Actin Binding Properties of Rabbit Skeletal Muscle .ALPHA.-Tropomyosin.

Sano Ken-Ichi,Maeda Kayo,Oda Toshiro,Maéda Yuichiro
The Journal of Biochemistry 127(6), 1095-1102, 2000
… Cosedimentation was employed to measure the cooperative actin binding of tropomyosin variants. …
NAID 130003533906

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