Melanophilin Polymorphism in Ferrets of Different Color
In mammals, the main contribution to the variability of pigmentation is made by two groups of genes directly related to the metabolic pathways of pigment synthesis and controlling the transport of melanosomes in melanocytes to keratinocytes. In order to identify the genetic basis of pigmentation var...
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Veröffentlicht in: | Doklady. Biochemistry and biophysics 2023-12, Vol.513 (Suppl 1), p.S12-S17 |
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creator | Kosovsky, G. Yu Glazko, V. I. Abramov, O. I. Glazko, T. T. |
description | In mammals, the main contribution to the variability of pigmentation is made by two groups of genes directly related to the metabolic pathways of pigment synthesis and controlling the transport of melanosomes in melanocytes to keratinocytes. In order to identify the genetic basis of pigmentation variants, the nucleotide sequences of the melanophilin gene were compared in two groups of ferrets—silver-colored and wild-type animals—using sequencing of 16 exons. In carriers of silver color, a single nucleotide deletion was detected in the 9th exon, leading to a shift in the reading frame and the formation of a stop codon downstream. The protein encoded by the mutant allele is almost completely devoid of the C terminal domain of the protein responsible for the contact of melanosomes with actin during their moving to the periphery of melanocytes, but it retains the leading domain involved in the formation of melanosomes. The combination of the preservation of the N domain and the defect of the C domain of the mutant protein for the first time makes it possible to explain the incomplete dominance of the wild-type protein in heterozygotes. |
doi_str_mv | 10.1134/S1607672923700655 |
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Yu ; Glazko, V. I. ; Abramov, O. I. ; Glazko, T. T.</creator><creatorcontrib>Kosovsky, G. Yu ; Glazko, V. I. ; Abramov, O. I. ; Glazko, T. T.</creatorcontrib><description>In mammals, the main contribution to the variability of pigmentation is made by two groups of genes directly related to the metabolic pathways of pigment synthesis and controlling the transport of melanosomes in melanocytes to keratinocytes. In order to identify the genetic basis of pigmentation variants, the nucleotide sequences of the melanophilin gene were compared in two groups of ferrets—silver-colored and wild-type animals—using sequencing of 16 exons. In carriers of silver color, a single nucleotide deletion was detected in the 9th exon, leading to a shift in the reading frame and the formation of a stop codon downstream. The protein encoded by the mutant allele is almost completely devoid of the C terminal domain of the protein responsible for the contact of melanosomes with actin during their moving to the periphery of melanocytes, but it retains the leading domain involved in the formation of melanosomes. The combination of the preservation of the N domain and the defect of the C domain of the mutant protein for the first time makes it possible to explain the incomplete dominance of the wild-type protein in heterozygotes.</description><identifier>ISSN: 1607-6729</identifier><identifier>EISSN: 1608-3091</identifier><identifier>DOI: 10.1134/S1607672923700655</identifier><identifier>PMID: 38189891</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>Actin ; Animals ; Biochemistry ; Biological and Medical Physics ; Biomedical and Life Sciences ; Biophysics ; Exons ; Ferrets - genetics ; Gene deletion ; Heterozygotes ; Keratinocytes ; Life Sciences ; Melanocytes ; Melanocytes - metabolism ; Melanosomes ; Melanosomes - genetics ; Melanosomes - metabolism ; Metabolic pathways ; Mutants ; Pigmentation ; Proteins ; Silver - metabolism ; Stop codon</subject><ispartof>Doklady. 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T.</creatorcontrib><title>Melanophilin Polymorphism in Ferrets of Different Color</title><title>Doklady. Biochemistry and biophysics</title><addtitle>Dokl Biochem Biophys</addtitle><addtitle>Dokl Biochem Biophys</addtitle><description>In mammals, the main contribution to the variability of pigmentation is made by two groups of genes directly related to the metabolic pathways of pigment synthesis and controlling the transport of melanosomes in melanocytes to keratinocytes. In order to identify the genetic basis of pigmentation variants, the nucleotide sequences of the melanophilin gene were compared in two groups of ferrets—silver-colored and wild-type animals—using sequencing of 16 exons. In carriers of silver color, a single nucleotide deletion was detected in the 9th exon, leading to a shift in the reading frame and the formation of a stop codon downstream. The protein encoded by the mutant allele is almost completely devoid of the C terminal domain of the protein responsible for the contact of melanosomes with actin during their moving to the periphery of melanocytes, but it retains the leading domain involved in the formation of melanosomes. The combination of the preservation of the N domain and the defect of the C domain of the mutant protein for the first time makes it possible to explain the incomplete dominance of the wild-type protein in heterozygotes.</description><subject>Actin</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biological and Medical Physics</subject><subject>Biomedical and Life Sciences</subject><subject>Biophysics</subject><subject>Exons</subject><subject>Ferrets - genetics</subject><subject>Gene deletion</subject><subject>Heterozygotes</subject><subject>Keratinocytes</subject><subject>Life Sciences</subject><subject>Melanocytes</subject><subject>Melanocytes - metabolism</subject><subject>Melanosomes</subject><subject>Melanosomes - genetics</subject><subject>Melanosomes - metabolism</subject><subject>Metabolic pathways</subject><subject>Mutants</subject><subject>Pigmentation</subject><subject>Proteins</subject><subject>Silver - metabolism</subject><subject>Stop codon</subject><issn>1607-6729</issn><issn>1608-3091</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kDFPwzAQhS0EoqXwA1hQJBaWgM9OYntEhQJSEUjAHDnJGVIlcbGTof8elxaQQEx35_ve8-kRcgz0HIAnF0-QUZEJphgXlGZpukPG4UnGnCrY_exFvN6PyIH3C0oZZTzdJyMuQSqpYEzEPTa6s8u3uqm76NE2q9a6MPk2CvMMncPeR9ZEV7Ux6LDro6ltrDske0Y3Ho-2dUJeZtfP09t4_nBzN72cxyVnSR-nGmhRccY5BcNMkhqoClWKQqAuNIBErrWRJq1kBiCAM8hUmslECKk0IJ-Qs43v0tn3AX2ft7UvsQlHox18zlQwSYJGBvT0F7qwg-vCdYESPMSj2JqCDVU6671Dky9d3Wq3yoHm61TzP6kGzcnWeSharL4VXzEGgG0AH1bdK7qfr_93_QCh337o</recordid><startdate>20231201</startdate><enddate>20231201</enddate><creator>Kosovsky, G. Yu</creator><creator>Glazko, V. I.</creator><creator>Abramov, O. I.</creator><creator>Glazko, T. T.</creator><general>Pleiades Publishing</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20231201</creationdate><title>Melanophilin Polymorphism in Ferrets of Different Color</title><author>Kosovsky, G. Yu ; Glazko, V. I. ; Abramov, O. I. ; Glazko, T. T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c324t-5a10bd323301f2f45f1db9c7b7eaba118e3aaf8f5d8611713216956847789a1e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Actin</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Biological and Medical Physics</topic><topic>Biomedical and Life Sciences</topic><topic>Biophysics</topic><topic>Exons</topic><topic>Ferrets - genetics</topic><topic>Gene deletion</topic><topic>Heterozygotes</topic><topic>Keratinocytes</topic><topic>Life Sciences</topic><topic>Melanocytes</topic><topic>Melanocytes - metabolism</topic><topic>Melanosomes</topic><topic>Melanosomes - genetics</topic><topic>Melanosomes - metabolism</topic><topic>Metabolic pathways</topic><topic>Mutants</topic><topic>Pigmentation</topic><topic>Proteins</topic><topic>Silver - metabolism</topic><topic>Stop codon</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kosovsky, G. 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Biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kosovsky, G. Yu</au><au>Glazko, V. I.</au><au>Abramov, O. I.</au><au>Glazko, T. T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Melanophilin Polymorphism in Ferrets of Different Color</atitle><jtitle>Doklady. Biochemistry and biophysics</jtitle><stitle>Dokl Biochem Biophys</stitle><addtitle>Dokl Biochem Biophys</addtitle><date>2023-12-01</date><risdate>2023</risdate><volume>513</volume><issue>Suppl 1</issue><spage>S12</spage><epage>S17</epage><pages>S12-S17</pages><issn>1607-6729</issn><eissn>1608-3091</eissn><abstract>In mammals, the main contribution to the variability of pigmentation is made by two groups of genes directly related to the metabolic pathways of pigment synthesis and controlling the transport of melanosomes in melanocytes to keratinocytes. In order to identify the genetic basis of pigmentation variants, the nucleotide sequences of the melanophilin gene were compared in two groups of ferrets—silver-colored and wild-type animals—using sequencing of 16 exons. In carriers of silver color, a single nucleotide deletion was detected in the 9th exon, leading to a shift in the reading frame and the formation of a stop codon downstream. The protein encoded by the mutant allele is almost completely devoid of the C terminal domain of the protein responsible for the contact of melanosomes with actin during their moving to the periphery of melanocytes, but it retains the leading domain involved in the formation of melanosomes. 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subjects | Actin Animals Biochemistry Biological and Medical Physics Biomedical and Life Sciences Biophysics Exons Ferrets - genetics Gene deletion Heterozygotes Keratinocytes Life Sciences Melanocytes Melanocytes - metabolism Melanosomes Melanosomes - genetics Melanosomes - metabolism Metabolic pathways Mutants Pigmentation Proteins Silver - metabolism Stop codon |
title | Melanophilin Polymorphism in Ferrets of Different Color |
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