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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
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