DYNLL1

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DYNLL1
Protein DYNLL1 PDB 1cmi.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDYNLL1, DLC1, DLC8, DNCL1, DNCLC1, LC8, LC8a, PIN, hdlc1, dynein light chain LC8-type 1
External IDsMGI: 1861457 HomoloGene: 133063 GeneCards: DYNLL1
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for DYNLL1
Genomic location for DYNLL1
Band12q24.31Start120,469,850 bp[1]
End120,498,493 bp[1]
RNA expression pattern
PBB GE DYNLL1 200703 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003746
NM_001037494
NM_001037495

NM_019682

RefSeq (protein)

NP_001032583
NP_001032584
NP_003737

NP_062656

Location (UCSC)Chr 12: 120.47 – 120.5 MbChr 5: 115.3 – 115.3 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Dynein light chain 1, cytoplasmic is a protein that in humans is encoded by the DYNLL1 gene.[5][6][7][8]

Function[edit]

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.[8]

Interactions[edit]

DYNLL1 has been shown to interact with:

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000088986 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000009013 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:".
  4. ^ "Mouse PubMed Reference:".
  5. ^ Dick T, Ray K, Salz HK, Chia W (May 1996). "Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster". Molecular and Cellular Biology. 16 (5): 1966–77. doi:10.1128/mcb.16.5.1966. PMC 231184. PMID 8628263.
  6. ^ Jaffrey SR, Snyder SH (Nov 1996). "PIN: an associated protein inhibitor of neuronal nitric oxide synthase". Science. 274 (5288): 774–7. doi:10.1126/science.274.5288.774. PMID 8864115.
  7. ^ Pfister KK, Fisher EM, Gibbons IR, Hays TS, Holzbaur EL, McIntosh JR, Porter ME, Schroer TA, Vaughan KT, Witman GB, King SM, Vallee RB (Nov 2005). "Cytoplasmic dynein nomenclature". The Journal of Cell Biology. 171 (3): 411–3. doi:10.1083/jcb.200508078. PMC 2171247. PMID 16260502.
  8. ^ a b "Entrez Gene: DYNLL1 dynein, light chain, LC8-type 1".
  9. ^ Day CL, Puthalakath H, Skea G, Strasser A, Barsukov I, Lian LY, Huang DC, Hinds MG (Feb 2004). "Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands". The Biochemical Journal. 377 (Pt 3): 597–605. doi:10.1042/BJ20031251. PMC 1223895. PMID 14561217.
  10. ^ a b Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R (Jun 2004). "Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes". Cancer Cell. 5 (6): 575–85. doi:10.1016/j.ccr.2004.05.022. PMID 15193260.
  11. ^ a b c Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, Sheng M (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. 20 (12): 4524–34. doi:10.1523/JNEUROSCI.20-12-04524.2000. PMID 10844022.
  12. ^ Diefenbach RJ, Diefenbach E, Douglas MW, Cunningham AL (Dec 2002). "The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23". Biochemistry. 41 (50): 14906–15. doi:10.1021/bi026417u. PMID 12475239.
  13. ^ Crépieux P, Kwon H, Leclerc N, Spencer W, Richard S, Lin R, Hiscott J (Dec 1997). "I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain". Molecular and Cellular Biology. 17 (12): 7375–85. doi:10.1128/MCB.17.12.7375. PMC 232593. PMID 9372968.
  14. ^ Herzig RP, Andersson U, Scarpulla RC (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. 113 (23): 4263–73. PMID 11069771.
  15. ^ Lo KW, Kan HM, Chan LN, Xu WG, Wang KP, Wu Z, Sheng M, Zhang M (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. 280 (9): 8172–9. doi:10.1074/jbc.M411408200. PMID 15611139.

Further reading[edit]