Role of the exon 11 of the insulin receptor gene on insulin binding identified by anti-peptide antibodies

1994 ◽  
Vol 101 (1-2) ◽  
pp. 121-127 ◽  
Author(s):  
Giorgio Sesti ◽  
Antonella Nadia Tullio ◽  
Maria Adelaide Marini ◽  
Ernesto Manera ◽  
Patrizia Borboni ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Receptor Gene ◽  
Insulin Binding ◽  
Insulin Receptor Gene ◽  
Exon 11 ◽  
Peptide Antibodies

Evidence for tissue-specific alternative splicing of the ovine insulin receptor gene

1998 ◽  
Vol 1998 ◽  
pp. 96-96
Author(s):  
P.D. McGrattan ◽  
A.R.G. Wylie ◽  
A.J. Bjourson
Keyword(s):  
Alternative Splicing ◽  
Insulin Receptor ◽  
Receptor Gene ◽  
Protein Isoforms ◽  
Common Mechanism ◽  
Mrna Transcript ◽  
Insulin Receptor Gene ◽  
Tissue Specific ◽  
Specific Regulation ◽  
Exon 11

Alternative splicing of a discrete 36 base pair segment (exon 11) of the human and rat insulin receptor leads to the formation of high and low affinity isoforms differing as much as 3-fold in affinity for insulin. Alternative splicing is a common mechanism for generating protein isoforms and is often regulated in a tissue-specific fashion (Seino & Bell, 1989; Mosthaf et al., 1990). In humans, the lower affinity (B-isoform) mRNA transcript is predominantly expressed in tissues that are important for modulating glucose homeostasis such as the liver and muscle whereas the higher affinity (A-isoform) mRNA transcript is predominantly expressed in haematopoietic tissues such as spleen. Alternative splicing of the region of the ovine insulin receptor gene encoding exon 11 has recently been demonstrated (McGrattan et al., unpublished). The objective of the present study was to establish whether tissue-specific regulation of alternative splicing of the insulin receptor gene occurs in the ruminant animal.

Evidence for tissue-specific alternative splicing of the ovine insulin receptor gene

1998 ◽  
Vol 1998 ◽  
pp. 96-96
Author(s):  
P.D. McGrattan ◽  
A.R.G. Wylie ◽  
A.J. Bjourson
Keyword(s):  
Alternative Splicing ◽  
Insulin Receptor ◽  
Receptor Gene ◽  
Protein Isoforms ◽  
Common Mechanism ◽  
Mrna Transcript ◽  
Insulin Receptor Gene ◽  
Tissue Specific ◽  
Specific Regulation ◽  
Exon 11

Alternative splicing of a discrete 36 base pair segment (exon 11) of the human and rat insulin receptor leads to the formation of high and low affinity isoforms differing as much as 3-fold in affinity for insulin. Alternative splicing is a common mechanism for generating protein isoforms and is often regulated in a tissue-specific fashion (Seino & Bell, 1989; Mosthaf et al., 1990). In humans, the lower affinity (B-isoform) mRNA transcript is predominantly expressed in tissues that are important for modulating glucose homeostasis such as the liver and muscle whereas the higher affinity (A-isoform) mRNA transcript is predominantly expressed in haematopoietic tissues such as spleen. Alternative splicing of the region of the ovine insulin receptor gene encoding exon 11 has recently been demonstrated (McGrattan et al., unpublished). The objective of the present study was to establish whether tissue-specific regulation of alternative splicing of the insulin receptor gene occurs in the ruminant animal.

scholarly journals hnRNP A1 and hnRNP F Modulate the Alternative Splicing of Exon 11 of the Insulin Receptor Gene

PLoS ONE ◽  
2011 ◽  
Vol 6 (11) ◽  
pp. e27869 ◽  
Author(s):  
Indrani Talukdar ◽  
Supriya Sen ◽  
Rodolfo Urbano ◽  
James Thompson ◽  
John R. Yates ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Insulin Receptor ◽  
Receptor Gene ◽  
Hnrnp A1 ◽  
Insulin Receptor Gene ◽  
Hnrnp F ◽  
Exon 11

scholarly journals Neofunctionalization of a second insulin receptor gene in the wing-dimorphic planthopper, Nilaparvata lugens

PLoS Genetics ◽  
2021 ◽  
Vol 17 (6) ◽  
pp. e1009653
Author(s):  
Wen-Hua Xue ◽  
Nan Xu ◽  
Sun-Jie Chen ◽  
Xin-Yang Liu ◽  
Jin-Li Zhang ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Direct Evidence ◽  
Receptor Gene ◽  
Brown Planthopper ◽  
Nilaparvata Lugens ◽  
Insulin Receptor Gene ◽  
Starvation Tolerance ◽  
Regulatory Complexity ◽  
Vein Patterning

A single insulin receptor (InR) gene has been identified and extensively studied in model species ranging from nematodes to mice. However, most insects possess additional copies of InR, yet the functional significance, if any, of alternate InRs is unknown. Here, we used the wing-dimorphic brown planthopper (BPH) as a model system to query the role of a second InR copy in insects. NlInR2 resembled the BPH InR homologue (NlInR1) in terms of nymph development and reproduction, but revealed distinct regulatory roles in fuel metabolism, lifespan, and starvation tolerance. Unlike a lethal phenotype derived from NlInR1 null, homozygous NlInR2 null mutants were viable and accelerated DNA replication and cell proliferation in wing cells, thus redirecting short-winged–destined BPHs to develop into long-winged morphs. Additionally, the proper expression of NlInR2 was needed to maintain symmetric vein patterning in wings. Our findings provide the first direct evidence for the regulatory complexity of the two InR paralogues in insects, implying the functionally independent evolution of multiple InRs in invertebrates.

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