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PMID:20347812

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Citation

Bacart, J, Leloire, A, Levoye, A, Froguel, P, Jockers, R and Couturier, C (2010) Evidence for leptin receptor isoforms heteromerization at the cell surface. FEBS Lett. 584:2213-7

Abstract

Leptin mediates its metabolic effects through several leptin receptor (LEP-R) isoforms. In humans, long (LEPRb) and short (LEPRa,c,d) isoforms are generated by alternative splicing. Most of leptin's effects are believed to be mediated by the OB-Rb isoform. However, the role of short LEPR isoforms and the possible existence of heteromers between different isoforms are poorly understood. Using BRET1 and optimized co-immunoprecipitation, we observed LEPRa/b and LEPRb/c heteromers located at the plasma membrane and stabilized by leptin. Given the widespread coexpression of LEPRa and LEPRb, our results suggest that LEPRa/b heteromers may represent a major receptor species in most tissues.

Links

PubMed Online version:10.1016/j.febslet.2010.03.033

Keywords

Carrier Proteins/metabolism; Cell Membrane/metabolism; Cells/metabolism; Humans; Immunoprecipitation; Leptin/metabolism; Protein Isoforms/metabolism; Receptors, Leptin

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:LEPR

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P48357-3

F

Seeded From UniProt

complete

HUMAN:LEPR

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P48357-1

F

Seeded From UniProt

complete

Notes

See also

References

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