Cited by 164Developmental Biology and Gene RegulationGenomics and Chromatin DynamicsProtein Structure and Dynamics

The Nuclear LIM Domain Interactor NLI Mediates Homo- and Heterodimerization of LIM Domain Transcription Factors

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Jurata, Linda W., Pfaff, Samuel L., Gill, Gordon N.·1998·Journal of Biological Chemistry

Abstract

LIM domain-containing transcription factors are required for embryonic survival and for the determination of many cell types. The combinatorial expression of the LIM homeodomain proteins Isl1, Isl2, Lhx1, and Lhx3 in subsets of developing motor neurons correlates with the future organization of these neurons into motor columns with distinct innervation targets, implying a functional role for LIM homeodomain protein combinations in the specification of neuronal identity. NLI is a widely expressed, dimeric protein that has been shown to specifically interact with the LIM domains of LIM domain-containing transcription factors. The present studies demonstrate that NLI mediates homo- and heteromeric complex formation between LIM domain transcription factors, requiring both the N-terminal dimerization and C-terminal LIM interaction domains of NLI. Although the interaction between most LIM homeodomain proteins is dependent on NLI, a direct interaction between the LIM domains of Lhx3 and the homeodomains of Isl1 and Isl2 was also observed. This interaction was disrupted by NLI, demonstrating that the conformational state of Lhx3-Isl1/Isl2 complexes is modified by NLI. Evidence indicating that NLI facilitates long range enhancer-promoter interactions suggests that NLI-dependent LIM domain transcription factor complexes are involved in communication between transcriptional control elements.

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Crossref · 10.1074/jbc.273.6.3152

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  • LDB1 is a dimeric cofactor that does not have direct DNA-binding capacity, but interacts with the LIM domain of other TFs to form multi-protein complexes.

    “LIM domain-binding protein 1 (LDB1) is a dimeric cofactor that does not have direct DNA-binding capacity, but interacts with the LIM domain of other TFs to form multi-protein complexes [370].”

    From Transcriptional enhancers and their communication with gene promoters (2021) · cites this paper as [370]

    The Abstract identifies NLI as Ldb1 and describes its homodimerization and LIM-interaction domains. The Results report that NLI dimers link LIM-domain transcription factors in tetrameric complexes. Our copy does not establish the separate claim that Ldb1 has no direct DNA-binding capacity. (LLM, conf=0.84)

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Research works printed but not linked: 4

  1. Boehm, T., Foroni, L., Kaneko, Y., Perutz, M. F., and Rabbitts, T. H. (1991) Proc. Natl. Acad. Sci. U. S. A. 88, 4367-4371
  2. Jurata, L. W., Kenny, D. A., and Gill, G. N. (1996) Proc. Natl. Acad. Sci.
  3. Lai, J. S., and Herr, W. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 6958 -6962
  4. Bach, I., Rhodes, S. J., Pearse, R. V., II, Heinzel, T., Gloss, B., Scully, K. M., Sawchenko, P. E., and Rosenfeld, M. G. (1995) Proc. Natl. Acad. Sci.

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Authors
Jurata, L. W., Pfaff, S. L., & Gill, G. N.
Affiliations
  • University of California San Diego (US)
  • Salk Institute for Biological Studies (US)
Corresponding author
Gill, Gordon N.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-02
Volume
273
Issue
6
Pages
3152-3157
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2011115644
Cited by
164
References
39
Citations by year
2025: 4 · 2024: 3 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 3 · 2018: 2 · 2017: 7 · 2016: 8 · 2015: 6 · 2014: 5 · 2013: 5 · 2012: 4
FWCI
5.36
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • McKnight Foundation
  • National Institutes of Health
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK13149, DK07541)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
LIM domain, LIM-homeodomain transcription factor, protein dimerization, Isl1, ISL2, LHX3, Lhx1, motor neuron specification, enhancer-promoter interactions, transcriptional regulation, protein-protein interaction
MeSH terms
Cell Line, Cell Nucleus, DNA-Binding Proteins, Humans, Motor Neurons, Protein Binding, Recombinant Proteins, Transcription Factors, Homeodomain Proteins, Dimerization, LIM Domain Proteins

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