author_facet Claessens, An
Weyn, Christine
Merregaert, Joseph
Claessens, An
Weyn, Christine
Merregaert, Joseph
author Claessens, An
Weyn, Christine
Merregaert, Joseph
spellingShingle Claessens, An
Weyn, Christine
Merregaert, Joseph
Cellular and Molecular Biology Letters
The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
Cell Biology
Molecular Biology
Biochemistry
author_sort claessens, an
spelling Claessens, An Weyn, Christine Merregaert, Joseph 1689-1392 Walter de Gruyter GmbH Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.2478/s11658-007-0052-8 <jats:title>Abstract</jats:title><jats:p>Mouse chondrolectin (chodl) was isolated out of the tail tip of four-day old 129/SvJ mice as a by-product of a PCR-based subtractive cDNA library screening. The gene is predominantly expressed in adult skeletal muscle, heart, testes and lungs and in embryonic stadia. Chodl is the mouse homologue of human chondrolectin (CHODL), a gene that encodes for a type Ia transmembrane protein and that is expressed in human testis, prostate, heart and skeletal muscle tissue. CHODL-splice variants (CHODL f, CHODL fΔE, CHODL ΔE) are detected in human leukocytes. The proteins of the chondrolectin family belong to the family of C-type lectins. As the members of this protein family are important for a wide array of biological processes, the function of chodl was investigated by searching for its protein interaction partners. The β-subunit of Rab geranylgeranyl transferase (Rabggtb) was isolated 8 times after a complete Sos recruitment system (SRS) screen with the cytoplasmic domain of chodl. The interaction was confirmed with in vitro transcription/translation and co-immunoprecipitation (co-IP) experiments.</jats:p> The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase Cellular and Molecular Biology Letters
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series Cellular and Molecular Biology Letters
source_id 49
title The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
title_unstemmed The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
title_full The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
title_fullStr The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
title_full_unstemmed The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
title_short The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
title_sort the cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
topic Cell Biology
Molecular Biology
Biochemistry
url http://dx.doi.org/10.2478/s11658-007-0052-8
publishDate 2008
physical
description <jats:title>Abstract</jats:title><jats:p>Mouse chondrolectin (chodl) was isolated out of the tail tip of four-day old 129/SvJ mice as a by-product of a PCR-based subtractive cDNA library screening. The gene is predominantly expressed in adult skeletal muscle, heart, testes and lungs and in embryonic stadia. Chodl is the mouse homologue of human chondrolectin (CHODL), a gene that encodes for a type Ia transmembrane protein and that is expressed in human testis, prostate, heart and skeletal muscle tissue. CHODL-splice variants (CHODL f, CHODL fΔE, CHODL ΔE) are detected in human leukocytes. The proteins of the chondrolectin family belong to the family of C-type lectins. As the members of this protein family are important for a wide array of biological processes, the function of chodl was investigated by searching for its protein interaction partners. The β-subunit of Rab geranylgeranyl transferase (Rabggtb) was isolated 8 times after a complete Sos recruitment system (SRS) screen with the cytoplasmic domain of chodl. The interaction was confirmed with in vitro transcription/translation and co-immunoprecipitation (co-IP) experiments.</jats:p>
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author Claessens, An, Weyn, Christine, Merregaert, Joseph
author_facet Claessens, An, Weyn, Christine, Merregaert, Joseph, Claessens, An, Weyn, Christine, Merregaert, Joseph
author_sort claessens, an
container_issue 2
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container_title Cellular and Molecular Biology Letters
container_volume 13
description <jats:title>Abstract</jats:title><jats:p>Mouse chondrolectin (chodl) was isolated out of the tail tip of four-day old 129/SvJ mice as a by-product of a PCR-based subtractive cDNA library screening. The gene is predominantly expressed in adult skeletal muscle, heart, testes and lungs and in embryonic stadia. Chodl is the mouse homologue of human chondrolectin (CHODL), a gene that encodes for a type Ia transmembrane protein and that is expressed in human testis, prostate, heart and skeletal muscle tissue. CHODL-splice variants (CHODL f, CHODL fΔE, CHODL ΔE) are detected in human leukocytes. The proteins of the chondrolectin family belong to the family of C-type lectins. As the members of this protein family are important for a wide array of biological processes, the function of chodl was investigated by searching for its protein interaction partners. The β-subunit of Rab geranylgeranyl transferase (Rabggtb) was isolated 8 times after a complete Sos recruitment system (SRS) screen with the cytoplasmic domain of chodl. The interaction was confirmed with in vitro transcription/translation and co-immunoprecipitation (co-IP) experiments.</jats:p>
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spelling Claessens, An Weyn, Christine Merregaert, Joseph 1689-1392 Walter de Gruyter GmbH Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.2478/s11658-007-0052-8 <jats:title>Abstract</jats:title><jats:p>Mouse chondrolectin (chodl) was isolated out of the tail tip of four-day old 129/SvJ mice as a by-product of a PCR-based subtractive cDNA library screening. The gene is predominantly expressed in adult skeletal muscle, heart, testes and lungs and in embryonic stadia. Chodl is the mouse homologue of human chondrolectin (CHODL), a gene that encodes for a type Ia transmembrane protein and that is expressed in human testis, prostate, heart and skeletal muscle tissue. CHODL-splice variants (CHODL f, CHODL fΔE, CHODL ΔE) are detected in human leukocytes. The proteins of the chondrolectin family belong to the family of C-type lectins. As the members of this protein family are important for a wide array of biological processes, the function of chodl was investigated by searching for its protein interaction partners. The β-subunit of Rab geranylgeranyl transferase (Rabggtb) was isolated 8 times after a complete Sos recruitment system (SRS) screen with the cytoplasmic domain of chodl. The interaction was confirmed with in vitro transcription/translation and co-immunoprecipitation (co-IP) experiments.</jats:p> The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase Cellular and Molecular Biology Letters
spellingShingle Claessens, An, Weyn, Christine, Merregaert, Joseph, Cellular and Molecular Biology Letters, The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase, Cell Biology, Molecular Biology, Biochemistry
title The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
title_full The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
title_fullStr The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
title_full_unstemmed The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
title_short The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
title_sort the cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
title_unstemmed The cytoplasmic domain of chondrolectin interacts with the β-subunit of rab geranylgeranyl transferase
topic Cell Biology, Molecular Biology, Biochemistry
url http://dx.doi.org/10.2478/s11658-007-0052-8