DYNLL1

Protein-coding gene in humans
DYNLL1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1CMI, 3ZKE, 3ZKF, 1F95, 1F3C, 1F96

Identifiers
AliasesDYNLL1, DLC1, DLC8, DNCL1, DNCLC1, LC8, LC8a, PIN, hdlc1, dynein light chain LC8-type 1
External IDsOMIM: 601562 MGI: 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]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for DYNLL1
Genomic location for DYNLL1
Band5|5 FStart115,435,169 bp[2]
End115,439,058 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • prefrontal cortex

  • frontal pole

  • cingulate gyrus

  • Brodmann area 9

  • bronchial epithelial cell

  • Brodmann area 10

  • middle frontal gyrus

  • amygdala

  • olfactory bulb

  • hypothalamus
Top expressed in
  • medial ganglionic eminence

  • endocardial cushion

  • maxillary prominence

  • condyle

  • spermatid

  • hair follicle

  • seminiferous tubule

  • abdominal wall

  • fossa

  • superior frontal gyrus
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein domain specific binding
  • protein C-terminus binding
  • protein binding
  • cytoskeletal motor activity
  • cytoskeletal protein binding
  • plus-end-directed microtubule motor activity
  • dynein intermediate chain binding
  • dynein light intermediate chain binding
  • enzyme binding
  • nitric-oxide synthase regulator activity
  • protein homodimerization activity
  • protein heterodimerization activity
  • scaffold protein binding
Cellular component
  • cytoplasm
  • cytosol
  • centrosome
  • membrane
  • plasma membrane
  • microtubule associated complex
  • ciliary tip
  • mitochondrion
  • dynein complex
  • COP9 signalosome
  • mitotic spindle
  • microtubule
  • cytoskeleton
  • extracellular exosome
  • nucleus
  • kinetochore
  • cytoplasmic dynein complex
  • cilium
  • tertiary granule membrane
  • ficolin-1-rich granule membrane
  • microtubule organizing center
  • secretory granule
  • axon cytoplasm
Biological process
  • regulation of transcription, DNA-templated
  • substantia nigra development
  • antigen processing and presentation of exogenous peptide antigen via MHC class II
  • transcription, DNA-templated
  • endoplasmic reticulum to Golgi vesicle-mediated transport
  • positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway
  • G2/M transition of mitotic cell cycle
  • microtubule-based process
  • intraciliary retrograde transport
  • viral process
  • negative regulation of phosphorylation
  • macroautophagy
  • apoptotic process
  • intraciliary transport involved in cilium assembly
  • neutrophil degranulation
  • motile cilium assembly
  • ciliary basal body-plasma membrane docking
  • positive regulation of non-motile cilium assembly
  • transport along microtubule
  • cilium assembly
  • sister chromatid cohesion
  • regulation of G2/M transition of mitotic cell cycle
  • transport
  • spermatid development
  • positive regulation of insulin secretion involved in cellular response to glucose stimulus
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8655

56455

Ensembl

ENSG00000088986

ENSMUSG00000009013

UniProt

P63167

P63168

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: 115.44 – 115.44 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

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

DYNLL1 has been shown to interact with:

References

  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:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  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. Bibcode:1996Sci...274..774J. doi:10.1126/science.274.5288.774. PMID 8864115. S2CID 46494691.
  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. PMC 6772433. 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. doi:10.1242/jcs.113.23.4263. 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

  • Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, Bieber FR, Morton CC (Sep 1994). "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics. 23 (1): 42–50. doi:10.1006/geno.1994.1457. PMID 7829101.
  • 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.
  • Tochio H, Ohki S, Zhang Q, Li M, Zhang M (Nov 1998). "Solution structure of a protein inhibitor of neuronal nitric oxide synthase". Nature Structural Biology. 5 (11): 965–9. doi:10.1038/2940. PMID 9808041. S2CID 28591803.
  • Rodríguez-Crespo I, Straub W, Gavilanes F, Ortiz de Montellano PR (Nov 1998). "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. doi:10.1006/abbi.1998.0928. PMID 9808772.
  • Fan JS, Zhang Q, Li M, Tochio H, Yamazaki T, Shimizu M, Zhang M (Dec 1998). "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. doi:10.1074/jbc.273.50.33472. PMID 9837926.
  • Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A (Mar 1999). "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. doi:10.1016/S1097-2765(00)80456-6. PMID 10198631.
  • Liang J, Jaffrey SR, Guo W, Snyder SH, Clardy J (Aug 1999). "Structure of the PIN/LC8 dimer with a bound peptide". Nature Structural Biology. 6 (8): 735–40. doi:10.1038/11501. PMID 10426949. S2CID 30155673.
  • Epstein E, Sela-Brown A, Ringel I, Kilav R, King SM, Benashski SE, Yisraeli JK, Silver J, Naveh-Many T (Feb 2000). "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. doi:10.1172/JCI8557. PMC 289163. PMID 10683380.
  • 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. PMC 6772433. PMID 10844022.
  • Jacob Y, Badrane H, Ceccaldi PE, Tordo N (Nov 2000). "Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein". Journal of Virology. 74 (21): 10217–22. doi:10.1128/JVI.74.21.10217-10222.2000. PMC 102062. PMID 11024152.
  • 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. doi:10.1242/jcs.113.23.4263. PMID 11069771.
  • Haraguchi K, Satoh K, Yanai H, Hamada F, Kawabuchi M, Akiyama T (Nov 2000). "The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase". Genes to Cells. 5 (11): 905–911. doi:10.1046/j.1365-2443.2000.00374.x. PMID 11122378. S2CID 37107139.
  • Lo KW, Naisbitt S, Fan JS, Sheng M, Zhang M (Apr 2001). "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. doi:10.1074/jbc.M010320200. PMID 11148209.
  • Yano H, Lee FS, Kong H, Chuang J, Arevalo J, Perez P, Sung C, Chao MV (Feb 2001). "Association of Trk neurotrophin receptors with components of the cytoplasmic dynein motor". The Journal of Neuroscience. 21 (3): RC125. doi:10.1523/JNEUROSCI.21-03-j0003.2001. PMC 6762309. PMID 11157096.
  • Fan J, Zhang Q, Tochio H, Li M, Zhang M (Feb 2001). "Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain". Journal of Molecular Biology. 306 (1): 97–108. doi:10.1006/jmbi.2000.4374. PMID 11178896.
  • Bielli A, Thörnqvist PO, Hendrick AG, Finn R, Fitzgerald K, McCaffrey MW (Mar 2001). "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. doi:10.1006/bbrc.2001.4468. PMID 11243854.
  • Yu J, Yu L, Chen Z, Zheng L, Chen X, Wang X, Ren D, Zhao S (Mar 2002). "Protein inhibitor of neuronal nitric oxide synthase interacts with protein kinase A inhibitors". Brain Research. Molecular Brain Research. 99 (2): 145–9. doi:10.1016/S0169-328X(02)00104-3. PMID 11978406.
  • Fuhrmann JC, Kins S, Rostaing P, El Far O, Kirsch J, Sheng M, Triller A, Betz H, Kneussel M (Jul 2002). "Gephyrin interacts with Dynein light chains 1 and 2, components of motor protein complexes". The Journal of Neuroscience. 22 (13): 5393–402. doi:10.1523/JNEUROSCI.22-13-05393.2002. PMC 6758200. 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.
  • v
  • t
  • e
  • 1cmi: STRUCTURE OF THE HUMAN PIN/LC8 DIMER WITH A BOUND PEPTIDE
    1cmi: STRUCTURE OF THE HUMAN PIN/LC8 DIMER WITH A BOUND PEPTIDE
  • 1f3c: REFINED SOLUTION STRUCTURE OF 8KDA DYNEIN LIGHT CHAIN (DLC8)
    1f3c: REFINED SOLUTION STRUCTURE OF 8KDA DYNEIN LIGHT CHAIN (DLC8)
  • 1f95: SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX
    1f95: SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX
  • 1f96: SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND NNOS PEPTIDE COMPLEX
    1f96: SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND NNOS PEPTIDE COMPLEX
  • 1pwj: Structure of the Monomeric 8-kDa Dynein Light Chain and Mechanism of Domain Swapped Dimer Assembly
    1pwj: Structure of the Monomeric 8-kDa Dynein Light Chain and Mechanism of Domain Swapped Dimer Assembly
  • 1pwk: Structure of the Monomeric 8-kDa Dynein Light Chain and Mechanism of Domain Swapped Dimer Assembly
    1pwk: Structure of the Monomeric 8-kDa Dynein Light Chain and Mechanism of Domain Swapped Dimer Assembly
  • 1re6: Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic Ligands
    1re6: Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic Ligands
  • 1rhw: The solution structure of the pH-induced monomer of dynein light chain LC8 from Drosophila
    1rhw: The solution structure of the pH-induced monomer of dynein light chain LC8 from Drosophila
  • 2pg1: Structural analysis of a cytoplasmic dynein Light Chain-Intermediate Chain complex
    2pg1: Structural analysis of a cytoplasmic dynein Light Chain-Intermediate Chain complex