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O Lohi

Publications and source records attributed to O Lohi.

13 recordsLinked to original sources
PubMed2000

Vear, a novel Golgi-associated protein with VHS and gamma-adaptin "ear" domains.

The molecular basis of the selectivity and the details of the vesicle formation in endocytic and secretory pathways are still poorly known and most probably involve as yet unidentified components. Here we describe the cloning, expression, and tissue and cell distribution of a novel protein of 67 kDa (called Vear) that bears homology to several endocytosis-associated proteins in that it has a VHS domain in its N terminus. It is also similar to gamma-adaptin, the heavy subunit of AP-1, in having in its C terminus a typical "ear" domain. In immunofluorescence microscopy, Vear was seen in the Golgi complex as judged by a typical distribution pattern, a distinct colocalization with the Golgi marker gamma-adaptin, and a sensitivity to treatment of cells with brefeldin A. In cell fractionation, Vear partitioned with the post-nuclear membrane fraction. In transfection experiments, hemagglutinin-tagged full-length Vear and truncated Vear lacking the VHS domain assembled on and caused compaction of the Golgi complex. Golgi association without compaction was seen with the ear domain of Vear, whereas the VHS domain alone showed a diffuse membrane- and vesicle-associated distribution. The Golgi association and the bipartite structure along with the differential targeting of its domains suggest that Vear is involved in heterotypic vesicle/suborganelle interactions associated with the Golgi complex. Tissue-specific function of Vear is suggested by its high level of expression in kidney, muscle, and heart.

Adaptor Protein Complex gamma Subunits↗
PubMed1998

VHS domain marks a group of proteins involved in endocytosis and vesicular trafficking.

Endocytosis is driven by a mechanism which is characterized by an orderly congregation of a large number of proteins which effectuate, first, formation of a coated vesicles, second, pinching off the vesicle and, third, regulated transport. True to the nature of many other proteins involved in multimolecular complexes, also endocytosis-associated proteins, such as Eps15, clathrin and AP-2, are characterized by distinct domains which mediate the protein-protein interactions. We now report that a group of well-established endocytosis and/or vesicular trafficking proteins possess a VHS domain, a recently described domain with an unknown function. We suggest that in these proteins VHS serves as a membrane targeting domain which by its specific features together with FYVE, SH3 and/or TAM domains, which are also present in some VHS-containing proteins, is involved in the stage-specific assembly of the endocytic machinery.

Amino Acid Sequence↗
PubMed1998

EAST, a novel EGF receptor substrate, associates with focal adhesions and actin fibers.

EAST is a novel epidermal growth factor receptor (EGFR) substrate. It interacts with Eps15, another EGFR substrate which is involved in receptor endocytosis. In this study we show that EAST associates with focal adhesions and actin filaments. First, in immunofluorescence and electron microscopy analysis, an extensive codistribution of EAST with vinculin, paxillin and actin filaments was seen. Second, overexpression of the NH2 terminus of EAST led to a formation of actin-rich microspikes and membrane protrusions. Third, in cosedimentation assay EAST showed a direct association with actin. These results suggest that EAST is involved in the EGFR-regulated reorganization of the actin cytoskeleton and may be part of a link between cytoskeleton and endocytic machinery.

Actins↗
PubMed1998

EAST, an epidermal growth factor receptor- and Eps15-associated protein with Src homology 3 and tyrosine-based activation motif domains.

We describe the cloning and characterization of a new cytoplasmic protein designated epidermal growth factor receptor-associated protein with SH3- and TAM domains (EAST). It contains an Src homology 3 domain in its midregion and a tyrosine-based activation motif in its COOH terminus. Antibodies to EAST recognize a 68-kDa protein that is present in most chicken tissues. An epidermal growth factor (EGF)-dependent association between the EGF receptor (EGFR) and EAST was shown by reciprocal immunoprecipitation/immunoblotting studies with specific antibodies. Activated EGFR catalyzed the tyrosine phosphorylation of EAST, as judged by an in vitro kinase assay with both immunoprecipitated and purified EGFR. Immunoprecipitation/immunoblotting experiments also demonstrated an association between EAST and eps15, an EGFR substrate associated with clathrin-coated pits and vesicles, which is essential in the endocytotic pathway. The association between EAST and eps15 was not affected by EGF treatment. In immunofluorescence microscopy, EAST was shown to partially colocalize with clathrin. The sequence of the NH2-terminal portion of EAST shows a high degree of similarity with a group of proteins involved in endocytosis or vesicle trafficking. Thus, EAST is a novel signal transduction component probably involved in EGF signaling and in the endocytotic machinery.

Amino Acid Sequence↗
PubMed1998

Src phosphorylates EAST, a novel EGF receptor-associated protein.

We have recently found and characterized EAST, a novel EGF receptor-associated protein with SH3 and TAM domains. In this study we show that EAST becomes phosphorylated by Src kinase. This, in conjunction with our earlier observations on the close association between EAST and the endocytic machinery, suggests that EAST could be involved in Src-dependent effects on EGF receptor endocytosis.

Animals↗
PubMed1994

Genetic models for the inheritance of the silver colour mutation of foxes.

We consider genetic models for the inheritance of the particular colour patterns of silver foxes. The models are evaluated by computation of statistical likelihoods based on observations of related foxes in extended pedigrees. Problems caused by incomplete paternity information are addressed by inferences based on phenotypic observations. The unreliability of subjective evaluations of fur colour also provides difficulty, in particular crossfoxes emerge as being difficult to differentiate. No evidence of linkage between Agouti locus and Extension locus is found in this dataset.

Alleles↗
PubMed1992

Genetic polymorphism of esterase in plasma of American mink (Mustela vison L.).

Plasma samples of 412 minks, including 20 families and representing 15 lines, have been investigated by isoelectric focusing for the enzyme esterase (ES). The observed variation of the enzyme may be explained as a result of one locus with at least seven codominant alleles. The segregation of six alleles assumed for the locus in 20 families supports this genetic model. Genetic divergence among the lines is observed and may be due to founder effect and/or selection.

Alleles↗
PubMed1991

Genetic polymorphism of adenosine deaminase and mannose phosphate isomerase in blood of arctic foxes, Alopex lagopus.

Blood samples of 70 foxes, including 10 families, have been investigated by horizontal starch gel electrophoresis for the enzymes adenosine deaminase (ADA) and mannose phosphate isomerase (MPI). The observed variation of the enzymes could be explained as a result of one locus with two codominant alleles and one with three respectively. The segregation in the families of the alleles assumed for the two loci is in accordance with this genetic model. The frequency of the two alleles at the Ada locus is about the same and the slowest anodic migrating allele at the Mpi locus is the most frequent.

Adenosine Deaminase↗
PubMed1988

Genetic polymorphism of plasma alpha 1 B-glycoprotein and transferrin in arctic and silver foxes.

Plasma samples of 235 foxes from 38 complete families (14 of arctic foxes, 21 of silver foxes and 3 with arctic x silver fox hybrid offspring) were analysed by one-dimensional horizontal polyacrylamide gel electrophoresis (PAGE) pH 9.0 followed by general-protein staining of gels. A major postalbumin of fox plasma was identified as alpha 1B-glycoprotein (alpha 1B) by using immunoblotting with antiser m specific to human or pig plasma alpha 1B. Four codominant, autosomal alleles of alpha 1B were found in arctic foxes. Two transferrin (TF) alleles (TfF, TfS) were observed in arctic foxes and two (TfD, Tff) in silver foxes; the TF F type of both of the fox species showed identical electrophoretic mobilities. The arctic foxes showed a high degree of polymorphism for both TF and alpha 1B. The silver foxes showed a scarce polymorphism of TF and were monomorphic for alpha 1B. The arctic fox, silver fox and their hybrids could be clearly differentiated from one another by their plasma protein patterns obtained by the PAGE method.

Alleles↗