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Dynein, light chain, LC8-type 1
Protein DYNLL1 PDB 1cmi.png
PDB rendering based on 1cmi.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols DYNLL1 ; DLC1; DLC8; DNCL1; DNCLC1; LC8; LC8a; PIN; hdlc1
External IDs OMIM601562 MGI1861457 HomoloGene133063 GeneCards: DYNLL1 Gene
RNA expression pattern
PBB GE DYNLL1 200703 at tn.png
More reference expression data
Species Human Mouse
Entrez 8655 56455
Ensembl ENSG00000088986 ENSMUSG00000009013
UniProt P63167 P63168
RefSeq (mRNA) NM_001037494 NM_019682
RefSeq (protein) NP_001032583 NP_062656
Location (UCSC) Chr 12:
120.91 – 120.94 Mb
Chr 5:
115.3 – 115.3 Mb
PubMed search [1] [2]

Dynein light chain 1, cytoplasmic is a protein that in humans is encoded by the DYNLL1 gene.[1][2][3][4]

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.[4]


DYNLL1 has been shown to interact with DLGAP1,[5] MYO5A,[5] DYNC1I1,[6] BCL2L11,[7][8] NRF1,[9] IκBα,[10] PAK1,[8] DLG4[5] and TP53BP1.[11]


  1. ^ Dick T, Ray K, Salz HK, Chia W (June 1996). "Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster". Mol Cell Biol 16 (5): 1966–77. PMC 231184. PMID 8628263. 
  2. ^ Jaffrey SR, Snyder SH (December 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. 
  3. ^ Pfister KK, Fisher EM, Gibbons IR, Hays TS, Holzbaur EL, McIntosh JR, Porter ME, Schroer TA, Vaughan KT, Witman GB, King SM, Vallee RB (November 2005). "Cytoplasmic dynein nomenclature". J Cell Biol 171 (3): 411–3. doi:10.1083/jcb.200508078. PMC 2171247. PMID 16260502. 
  4. ^ a b "Entrez Gene: DYNLL1 dynein, light chain, LC8-type 1". 
  5. ^ a b c Naisbitt, S; Valtschanoff J; Allison D W; Sala C; Kim E; Craig A M; Weinberg R J; Sheng M (June 2000). "Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein". J. Neurosci. (UNITED STATES) 20 (12): 4524–34. ISSN 0270-6474. PMID 10844022. 
  6. ^ Diefenbach, Russell J; Diefenbach Eve; Douglas Mark W; Cunningham Anthony L (December 2002). "The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23". Biochemistry (United States) 41 (50): 14906–15. doi:10.1021/bi026417u. ISSN 0006-2960. PMID 12475239. 
  7. ^ Day, Catherine L; Puthalakath Hamsa; Skea Gretchen; Strasser Andreas; Barsukov Igor; Lian Lu-Yun; Huang David C S; Hinds Mark G (February 2004). "Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands". Biochem. J. (England) 377 (Pt 3): 597–605. doi:10.1042/BJ20031251. PMC 1223895. PMID 14561217. 
  8. ^ a b Vadlamudi, Ratna K; Bagheri-Yarmand Rozita, Yang Zhibo, Balasenthil Seetharaman, Nguyen Diep, Sahin Aysegul A, den Hollander Petra, Kumar Rakesh (June 2004). "Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes". Cancer Cell (United States) 5 (6): 575–85. doi:10.1016/j.ccr.2004.05.022. ISSN 1535-6108. PMID 15193260. 
  9. ^ Herzig, R P; Andersson U; Scarpulla R C (December 2000). "Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila". J. Cell. Sci. (ENGLAND). 113 Pt 23: 4263–73. ISSN 0021-9533. PMID 11069771. 
  10. ^ Crépieux, P; Kwon H; Leclerc N; Spencer W; Richard S; Lin R; Hiscott J (December 1997). "I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain". Mol. Cell. Biol. (UNITED STATES) 17 (12): 7375–85. ISSN 0270-7306. PMC 232593. PMID 9372968. 
  11. ^ Lo, Kevin W-H; Kan Ho-Man; Chan Ling-Nga; Xu Wei-Guang; Wang Ke-Peng; Wu Zhenguo; Sheng Morgan; Zhang Mingjie (March 2005). "The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation". J. Biol. Chem. (United States) 280 (9): 8172–9. doi:10.1074/jbc.M411408200. ISSN 0021-9258. PMID 15611139. 

Further reading[edit]