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author Yang, Hao
Chen, Ting
Zhang, Xin
Zhou, Mingyu
Zhang, Lvping
Yan, Aifen
Chen, Weihao
Tan, Guiling
Liang, Jingxuan
Ren, Chunhua
Chen, Xiaoli
Li, Zhi
Ruan, Yao
Li, Jiaxi
Li, Hongmei
Luo, Peng
Wang, Yanhong
Jiang, Xiao
Yin, Jiayue
Ma, Bo
Zhu, Chunhua
Wu, Xugan
Zhang, Jiquan
Hu, Chaoqun
author_facet Yang, Hao
Chen, Ting
Zhang, Xin
Zhou, Mingyu
Zhang, Lvping
Yan, Aifen
Chen, Weihao
Tan, Guiling
Liang, Jingxuan
Ren, Chunhua
Chen, Xiaoli
Li, Zhi
Ruan, Yao
Li, Jiaxi
Li, Hongmei
Luo, Peng
Wang, Yanhong
Jiang, Xiao
Yin, Jiayue
Ma, Bo
Zhu, Chunhua
Wu, Xugan
Zhang, Jiquan
Hu, Chaoqun
Yang, Hao
Chen, Ting
Zhang, Xin
Zhou, Mingyu
Zhang, Lvping
Yan, Aifen
Chen, Weihao
Tan, Guiling
Liang, Jingxuan
Ren, Chunhua
Chen, Xiaoli
Li, Zhi
Ruan, Yao
Li, Jiaxi
Li, Hongmei
Luo, Peng
Wang, Yanhong
Jiang, Xiao
Yin, Jiayue
Ma, Bo
Zhu, Chunhua
Wu, Xugan
Zhang, Jiquan
Hu, Chaoqun
collection PubMed - marine biology
contents Crustacean methyl farnesoate-binding protein is an insect juvenile hormone-binding protein homolog that inhibits molting. Yang, Hao Chen, Ting Zhang, Xin Zhou, Mingyu Zhang, Lvping Yan, Aifen Chen, Weihao Tan, Guiling Liang, Jingxuan Ren, Chunhua Chen, Xiaoli Li, Zhi Ruan, Yao Li, Jiaxi Li, Hongmei Luo, Peng Wang, Yanhong Jiang, Xiao Yin, Jiayue Ma, Bo Zhu, Chunhua Wu, Xugan Zhang, Jiquan Hu, Chaoqun Animals Molting Fatty Acids, Unsaturated Insect Proteins Carrier Proteins Penaeidae Juvenile Hormones Hemolymph Amino Acid Sequence Hepatopancreas Arthropod Proteins Methyl farnesoate (MF) serves as an essential regulator of key developmental processes in crustaceans, similar to juvenile hormones (JHs) in insects. However, it is susceptible to degradation in circulation. Despite the detection of proteins binding to MF in crustacean hemolymph for 3 decades, the precise genes encoding these proteins remain unclear. The present study identifies genes in crustaceans containing the juvenile hormone-binding protein (JHBP) domain. Among the 11 JHBPs found in the Pacific white shrimp (Litopenaeus vannamei), XP_027209752.1, which is primarily expressed in the hepatopancreas, emerges as the predominant form. This protein exhibits selective binding to MF rather than to JHs, leading to its designation as a methyl farnesoate-binding protein (MFBP) in crustaceans. Alterations in the amino acid sequence are predicted to induce structural changes that enhance the affinity of MFBP for MF. Endogenous MFBP inhibits molting, consistent with the function of MF. Furthermore, positive regulation of MFBP by MF has been observed in hepatopancreatic primary cells, with similar trends of hepatopancreatic MFBP mRNA and hemolymph MF levels during molting and ovarian development. This study identifies a novel MFBP in crustaceans that, despite being a homolog of insect JHBP, specifically binds MF to regulate molting in penaeid shrimp. These findings may advance our understanding of crustacean endocrine regulation and provide a molecular basis for improving their aquaculture techniques.
format Artículo científico
id pubmed_40441536
institution PubMed
language en
publishDate 2025
publisher The Journal of biological chemistry
record_format pubmed
spellingShingle Crustacean methyl farnesoate-binding protein is an insect juvenile hormone-binding protein homolog that inhibits molting.
Yang, Hao
Chen, Ting
Zhang, Xin
Zhou, Mingyu
Zhang, Lvping
Yan, Aifen
Chen, Weihao
Tan, Guiling
Liang, Jingxuan
Ren, Chunhua
Chen, Xiaoli
Li, Zhi
Ruan, Yao
Li, Jiaxi
Li, Hongmei
Luo, Peng
Wang, Yanhong
Jiang, Xiao
Yin, Jiayue
Ma, Bo
Zhu, Chunhua
Wu, Xugan
Zhang, Jiquan
Hu, Chaoqun
Animals
Molting
Fatty Acids, Unsaturated
Insect Proteins
Carrier Proteins
Penaeidae
Juvenile Hormones
Hemolymph
Amino Acid Sequence
Hepatopancreas
Arthropod Proteins
Crustacean methyl farnesoate-binding protein is an insect juvenile hormone-binding protein homolog that inhibits molting. Yang, Hao Chen, Ting Zhang, Xin Zhou, Mingyu Zhang, Lvping Yan, Aifen Chen, Weihao Tan, Guiling Liang, Jingxuan Ren, Chunhua Chen, Xiaoli Li, Zhi Ruan, Yao Li, Jiaxi Li, Hongmei Luo, Peng Wang, Yanhong Jiang, Xiao Yin, Jiayue Ma, Bo Zhu, Chunhua Wu, Xugan Zhang, Jiquan Hu, Chaoqun Animals Molting Fatty Acids, Unsaturated Insect Proteins Carrier Proteins Penaeidae Juvenile Hormones Hemolymph Amino Acid Sequence Hepatopancreas Arthropod Proteins Methyl farnesoate (MF) serves as an essential regulator of key developmental processes in crustaceans, similar to juvenile hormones (JHs) in insects. However, it is susceptible to degradation in circulation. Despite the detection of proteins binding to MF in crustacean hemolymph for 3 decades, the precise genes encoding these proteins remain unclear. The present study identifies genes in crustaceans containing the juvenile hormone-binding protein (JHBP) domain. Among the 11 JHBPs found in the Pacific white shrimp (Litopenaeus vannamei), XP_027209752.1, which is primarily expressed in the hepatopancreas, emerges as the predominant form. This protein exhibits selective binding to MF rather than to JHs, leading to its designation as a methyl farnesoate-binding protein (MFBP) in crustaceans. Alterations in the amino acid sequence are predicted to induce structural changes that enhance the affinity of MFBP for MF. Endogenous MFBP inhibits molting, consistent with the function of MF. Furthermore, positive regulation of MFBP by MF has been observed in hepatopancreatic primary cells, with similar trends of hepatopancreatic MFBP mRNA and hemolymph MF levels during molting and ovarian development. This study identifies a novel MFBP in crustaceans that, despite being a homolog of insect JHBP, specifically binds MF to regulate molting in penaeid shrimp. These findings may advance our understanding of crustacean endocrine regulation and provide a molecular basis for improving their aquaculture techniques.
title Crustacean methyl farnesoate-binding protein is an insect juvenile hormone-binding protein homolog that inhibits molting.
topic Animals
Molting
Fatty Acids, Unsaturated
Insect Proteins
Carrier Proteins
Penaeidae
Juvenile Hormones
Hemolymph
Amino Acid Sequence
Hepatopancreas
Arthropod Proteins
url https://pubmed.ncbi.nlm.nih.gov/40441536/