Biology:LIM domain-binding protein family

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Short description: Family of proteins
LIM-domain binding protein
Identifiers
SymbolLIM_bind
PfamPF01803
InterProIPR002691
SCOP21j2o / SCOPe / SUPFAM

In molecular biology, the LIM domain-binding protein family is a family of proteins which binds to the LIM domain of LIM (LIN-11, Isl-1 and MEC-3) homeodomain proteins which are transcriptional regulators of development.

Examples

Nuclear LIM interactor (NLI) / LIM domain-binding protein 1 (LDB1) is located in the nuclei of neuronal cells during development, it is co-expressed with ISL1 in early motor neuron differentiation and has a suggested role in the ISL1 dependent development of motor neurons.[1] It is suggested that these proteins act synergistically to enhance transcriptional efficiency by acting as co-factors for LIM homeodomain and Otx class transcription factors both of which have essential roles in development.[2] The Drosophila melanogaster protein Chip is required for segmentation and activity of a remote wing margin enhancer.[3] Chip is a ubiquitous chromosomal factor required for normal expression of diverse genes at many stages of development.[3] It is suggested that Chip cooperates with different LIM domain proteins and other factors to structurally support remote enhancer-promoter interactions.[3]

References

  1. "Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting protein, is expressed early in neuronal development". Proc. Natl. Acad. Sci. U.S.A. 93 (21): 11693–8. October 1996. doi:10.1073/pnas.93.21.11693. PMID 8876198. Bibcode1996PNAS...9311693J. 
  2. "A family of LIM domain-associated cofactors confer transcriptional synergism between LIM and Otx homeodomain proteins". Genes Dev. 11 (11): 1370–80. June 1997. doi:10.1101/gad.11.11.1370. PMID 9192866. 
  3. 3.0 3.1 3.2 "Chip, a widely expressed chromosomal protein required for segmentation and activity of a remote wing margin enhancer in Drosophila". Genes Dev. 11 (20): 2729–40. October 1997. doi:10.1101/gad.11.20.2729. PMID 9334334. 
This article incorporates text from the public domain Pfam and InterPro: IPR002691