Biology:DYNLL1

Generic protein structure example

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:

• BCL2L11,
• DLG4
• DLGAP1,
• DYNC1I1,
• IκBα,
• MYO5A,
• NRF1,
• PAK1, and
• TP53BP1.

Further reading

• "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics 23 (1): 42–50. Sep 1994. doi:10.1006/geno.1994.1457. PMID 7829101. 
• "I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain". Molecular and Cellular Biology 17 (12): 7375–85. Dec 1997. doi:10.1128/MCB.17.12.7375. PMID 9372968. 
• "Solution structure of a protein inhibitor of neuronal nitric oxide synthase". Nature Structural Biology 5 (11): 965–9. Nov 1998. doi:10.1038/2940. PMID 9808041. 
• "Binding of dynein light chain (PIN) to neuronal nitric oxide synthase in the absence of inhibition". Archives of Biochemistry and Biophysics 359 (2): 297–304. Nov 1998. doi:10.1006/abbi.1998.0928. PMID 9808772. 
• "Protein inhibitor of neuronal nitric-oxide synthase, PIN, binds to a 17-amino acid residue fragment of the enzyme". The Journal of Biological Chemistry 273 (50): 33472–81. Dec 1998. doi:10.1074/jbc.273.50.33472. PMID 9837926. 
• "The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex". Molecular Cell 3 (3): 287–96. Mar 1999. doi:10.1016/S1097-2765(00)80456-6. PMID 10198631. 
• "Structure of the PIN/LC8 dimer with a bound peptide". Nature Structural Biology 6 (8): 735–40. Aug 1999. doi:10.1038/11501. PMID 10426949. 
• "Dynein light chain binding to a 3'-untranslated sequence mediates parathyroid hormone mRNA association with microtubules". The Journal of Clinical Investigation 105 (4): 505–12. Feb 2000. doi:10.1172/JCI8557. PMID 10683380. 
• "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 20 (12): 4524–34. Jun 2000. doi:10.1523/JNEUROSCI.20-12-04524.2000. PMID 10844022. 
• "Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein". Journal of Virology 74 (21): 10217–22. Nov 2000. doi:10.1128/JVI.74.21.10217-10222.2000. PMID 11024152. 
• "Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila". Journal of Cell Science 113 (23): 4263–73. Dec 2000. doi:10.1242/jcs.113.23.4263. PMID 11069771. 
• "The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase". Genes to Cells 5 (11): 905–911. Nov 2000. doi:10.1046/j.1365-2443.2000.00374.x. PMID 11122378. 
• "The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif". The Journal of Biological Chemistry 276 (17): 14059–66. Apr 2001. doi:10.1074/jbc.M010320200. PMID 11148209. 
• "Association of Trk neurotrophin receptors with components of the cytoplasmic dynein motor". The Journal of Neuroscience 21 (3): RC125. Feb 2001. doi:10.1523/JNEUROSCI.21-03-j0003.2001. PMID 11157096. 
• "Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain". Journal of Molecular Biology 306 (1): 97–108. Feb 2001. doi:10.1006/jmbi.2000.4374. PMID 11178896. 
• "The small GTPase Rab4A interacts with the central region of cytoplasmic dynein light intermediate chain-1". Biochemical and Biophysical Research Communications 281 (5): 1141–53. Mar 2001. doi:10.1006/bbrc.2001.4468. PMID 11243854. 
• "Protein inhibitor of neuronal nitric oxide synthase interacts with protein kinase A inhibitors". Brain Research. Molecular Brain Research 99 (2): 145–9. Mar 2002. doi:10.1016/S0169-328X(02)00104-3. PMID 11978406. 
• "Gephyrin interacts with Dynein light chains 1 and 2, components of motor protein complexes". The Journal of Neuroscience 22 (13): 5393–402. Jul 2002. doi:10.1523/JNEUROSCI.22-13-05393.2002. PMID 12097491. 

External links

• Overview of all the structural information available in the PDB for UniProt: P63167 (Dynein light chain 1, cytoplasmic) at the PDBe-KB.