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FLASH GENE
Symbol DYNLL1 contributors: mct/npt/pgu - updated : 01-03-2015
HGNC name dynein, light chain, LC8-type 1
HGNC id 15476
EXPRESSION
Type ubiquitous
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Digestiveliver   highly
 stomach   highly
Endocrinepancreas   highly
Urinarybladder   highly
cell lineage
cell lines
fluid/secretion
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • three potential C2H2 zinc finger structures
  • IKAROS-like motif
  • at least 18 SQ/TQ motifs in its sequence
  • mono polymer homomer , dimer
    HOMOLOGY
    Homologene
    FAMILY
  • dynein light chain family
  • CATEGORY motor/contractile
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm,organelle,mitochondria
    intracellular,cytoplasm,cytosolic
    intracellular,cytoplasm,cytoskeleton,microtubule,centrosome
    intracellular,cytoplasm,cytoskeleton,microtubule,mitotic spindle
    intracellular,nucleus,chromatin/chromosome,kinetochore
    basic FUNCTION
  • dynein light chain, may be involved in some aspects of dynein-related intracellular transport and motility
  • may play a role in changing or maintaining the spatial distribution of cytoskeletal structures
  • involved in fundamental processes, including retrograde vesicular trafficking, ciliary/flagellar motility, and cell division
  • having crucial regulatory roles, in various systems potentially due to its ability to promote dimerization of partially disordered proteins
  • DYNLL1, DYNLL2 are required for outer arm dynein motor function
  • is not required for NEK9 oligomerization
  • is not absolutely required for NEK9 autoactivation, but binding to NEK9 increases the efficiency of this process
  • acts as a hub protein in several cellular events having functions unrelated to cargo transport, for instance in nuclear transport, apoptosis and cancer development
  • DYNLL1 binding to certain cellular targets interferes with ATM/ATR phosphorylation and vice versa
  • required for the asymmetric cortical localization of dynein and has a specific function defining spindle orientation
  • positive regulator of DNA damage-related ATMIN functions, indicating that the functional interactions between the two proteins may be context-dependent
  • having microtubule-associated protein-like function that could explain its reported roles in cellular metastasis and differentiation
  • inhibits osteoclast differentiation by regulating NFKB and MAPK pathways
  • ARL3 and DYNLL1 regulate dissociation of dynactin from dynein
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • essential component of the microtubule-based molecular motor dynein
  • forms a stable homodimer
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • with TRPS1(suppression of transcriptional repression activity of TRPS1)
  • binding with BMF and BCL2L11
  • RASGRP3-interacting protein (represents a novel anchoring protein for RASGRP3 that may regulate subcellular localization of the exchange factor and, as such, may participate in the signaling mediated by diacylglycerol through RASGRP3)
  • also interacts with proteins that are not clearly connected with dynein or microtubule-based transport, including some with roles in apoptosis, viral pathogenesis, enzyme regulation, and kidney developmen
  • binds CHUK in a redox-dependent manner and thereby prevents its phosphorylation by IKK (TXNDC17 contributes to this inhibitory activity by maintaining DYNLL1 in a reduced state)
  • interacting partner of GNB2L1 (GNB2L1 formed a complex with DYNLL1 and BCL2L11, in the presence of apoptotic agents)
  • cooperate with PAK1 in malignant transformation of breast cancer cells (facilitates nuclear import of PAK1, function indispensable during vertebrate development)
  • DYNLL1 was identified as a new target of disulfide reductase activity of TXNDC17, and DYNLL1 was shown to bind IkappaBalpha in a redox-dependent manner, thereby preventing its phosphorylation by IKBKB
  • regulates syntaphilin-mediated mitochondrial docking in axons
  • POLR2M is a DYNLL1 binding partner
  • NEK9 binds to DYNLL/LC8, a highly conserved protein originally described as a component of the dynein complex (binding interferes with the interaction of NEK9 with its downstream partner NEK6 as well as with NEK6 activation, thus controlling both processes)
  • ATMIN is a DYNLL1-binding partner (DYNLL1 binds to multiple SQ/TQ motifs present in the C-terminal domain of ATMIN)
  • bind to proteins with KXTQT motifs
  • key role of ATMIN in regulating the survival of developing B cells by activating DYNLL1 expression, which may then modulate BCL2L11-dependent apoptosis
  • DYNLL1 interacted with a spindle-microtubule-associated adaptor formed by FAM83D and HMMR via TQT motifs in FAM83D)
  • binding to NEK9 was regulated by NEK9 autophosphorylation on Ser(944), a AA immediately located N-terminal to the DYNLL1 conserved (K/R)xTQT binding motif
  • WDR34 is a direct interaction partner of the cytoplasmic dynein-1 light chain DYNLL1
  • ATMIN primarily promotes ciliogenesis by regulating DYNLL1 expression
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    ANIMAL & CELL MODELS