DYNLL1

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Protein-coding gene in humans

title: "DYNLL1" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public description: "Protein-coding gene in humans" topic_path: "uncategorized" source: "https://en.wikipedia.org/wiki/DYNLL1" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in humans ::

Dynein light chain 1, cytoplasmic is a protein that in humans is encoded by the DYNLL1 gene.

Function

Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized.

Interactions

DYNLL1 has been shown to interact with:

References

References

  1. (May 1996). "Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster". Molecular and Cellular Biology.
  2. (Nov 1996). "PIN: an associated protein inhibitor of neuronal nitric oxide synthase". Science.
  3. (Nov 2005). "Cytoplasmic dynein nomenclature". The Journal of Cell Biology.
  4. "Entrez Gene: DYNLL1 dynein, light chain, LC8-type 1".
  5. (Feb 2004). "Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands". The Biochemical Journal.
  6. (Jun 2004). "Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes". Cancer Cell.
  7. (Jun 2000). "Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein". The Journal of Neuroscience.
  8. (Dec 2002). "The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23". Biochemistry.
  9. (Dec 1997). "I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain". Molecular and Cellular Biology.
  10. (Dec 2000). "Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila". Journal of Cell Science.
  11. (Mar 2005). "The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation". The Journal of Biological Chemistry.

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