DYNLL1

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

DYNLL1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1CMI, 3ZKE, 3ZKF, 1F95, 1F3C, 1F96
Identifiers
Aliases	DYNLL1, DLC1, DLC8, DNCL1, DNCLC1, LC8, LC8a, PIN, hdlc1, dynein light chain LC8-type 1
External IDs	OMIM: 601562; MGI: 1861457; HomoloGene: 133063; GeneCards: DYNLL1; OMA:DYNLL1 - orthologs
Gene location (Human) Chr. Chromosome 12 (human) Band 12q24.31 Start 120,469,850 bp End 120,498,493 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 F Start 115,435,169 bp End 115,439,058 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in prefrontal cortex frontal pole gingival epithelium cingulate gyrus anterior cingulate cortex Brodmann area 9 bronchial epithelial cell right testis Brodmann area 10 right frontal lobe Top expressed in medial ganglionic eminence endocardial cushion dentate gyrus of hippocampal formation granule cell maxillary prominence condyle mandibular prominence spermatid hair follicle seminiferous tubule abdominal wall 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 Species Human Mouse 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 Mb Chr 5: 115.44 – 115.44 Mb PubMed search
Wikidata
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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

• 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.