DYNLL/LC8: a light chain subunit of the dynein motor complex and beyond

Rapali, Péter; Szenes, Áron; Radnai, László; Bakos, Anita; Pál, Gábor; Nyitray, László

doi:10.1111/j.1742-4658.2011.08254.x

Cited by 132 publications

(207 citation statements)

References 136 publications

(187 reference statements)

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“…Lack of dynein heavy chains observed in Western blot indicates that in O. umbellatum lipotubuloids dynein light chains did not form dynein. They are core elements of eukaryotic cells probably binding with hundreds of proteins (Rapali et al 2011). The presence of dynein light chain molecules in fibroblast Golgi structures (Tai et al 1998) support our observations reaviling them by immunogold method as gold grains in lipotubuloid Golgi structures.…”

Section: Discussionsupporting

confidence: 76%

Immunogold method evidences that kinesin and myosin bind to and couple microtubules and actin filaments in lipotubuloids of Ornithogalum umbellatum ovary epidermis

et al. 2013

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Lipotubuloids in ovary epidermis of Ornithogalum umbellatum which are a domain of cytoplasm containing a lot of lipid bodies, microtubules and actin filaments, ribosomes, endoplasmic reticulum as well as scarce mitochondria, microbodies, dictyosomes, autolytic vacuoles, exhibit progressive-rotary motion. The immunogold method demonstrated that microtubules and actin filaments of lipotubuloids might be connected with one another by myosin and kinesin. It was supposed that collaboration of motor proteins with actin filaments and microtubules makes autonomic high peripheral speed rotary motion of lipotubuloids in epidermis cells possible. Moreover, myosin was also detected in Golgi bodies in lipotubuloid. In lipotubuloids, the immunogold method demonstrated immunosignals after the use of an antibody to dynein light chains but spectroscopy mass analysis showed that in O. umbellatum epidermis lacked dynein heavy chains.

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Section: Discussionsupporting

confidence: 76%

Immunogold method evidences that kinesin and myosin bind to and couple microtubules and actin filaments in lipotubuloids of Ornithogalum umbellatum ovary epidermis

et al. 2013

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“…18 Our study unravels an important function for the dynein light chain Tctex-1 at the kinetochore in a dynein independent manner. Evidence for this model includes the following.…”

Section: Discussionmentioning

confidence: 99%

“…Structural studies support a role for dynein light chains to promote protein dimerization and structural stabilization. 18 These light chains can allosterically bind to and regulate, besides dynein, diverse proteins and protein complexes. Future work will require the identification of the binding partner for the dyneinindependent population at kinetochores.…”

Section: Discussionmentioning

confidence: 99%

“…For example, the LC8 family members of dynein light chains have been shown to interact, besides dynein, with a large number of proteins. 18 Similarly, the Tctex family member of Tctex-1 (or DYNLT1) has dynein-independent roles in actin remodeling during neurite outgrowth 19 and in ciliary resorption. 20, 21 We now show that Tctex-1 associates with unattached kinetochores and participates in stable microtubule attachment independent of cytoplasmic dynein.…”

Section: Introductionmentioning

confidence: 99%

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A dynein independent role of Tctex-1 at the kinetochore

et al. 2015

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Dynein light chains are accessory subunits of the cytoplasmic dynein complex, a minus-end directed microtubule motor. Here, we demonstrate that the dynein light chain Tctex-1 associates with unattached kinetochores and is essential for accurate chromosome segregation. Tctex-1 knockdown in cells does not affect the localization and function of dynein at the kinetochore, but produces a prolonged mitotic arrest with a few misaligned chromosomes, which are subsequently missegregated during anaphase. This function is independent of Tctex-1's association with dynein. The kinetochore localization of Tctex-1 is independent of the ZW10-dynein pathway, but requires the Ndc80 complex. Thus, our findings reveal a dynein independent role of Tctex-1 at the kinetochore to enhance the stability of kinetochore-microtubule attachment.

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“…The LC8 dynein light chains were originally described as the smallest subunit of the microtubuleassociated cytoplasmic dynein motor complex.They show a highly conserved amino acid sequence throughout evolution and they were later shown to bind to more than 70 other proteins involved in various biological processes, therefore they are now considered hub proteins (1,2).Vertebrates contain two closely related LC8 paralogs, DYNLL1 and DYNLL2 with partially overlapping functions (1). Under physiological conditions LC8proteins arestable homodimers (3).Atomic resolution structureswere determined both for the apo and ligand-bound form using X-ray crystallographyand NMR spectroscopy (4)(5)(6).…”

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confidence: 99%

DYNLL2 Dynein Light Chain Binds to an Extended Linear Motif of Myosin 5a Tail That Has Structural Plasticity

Bodor¹,

Radnai²,

Hetényi

et al. 2014

Biochemistry

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LC8 dynein light chains (DYNLL) are conserved homodimeric eukaryotic hub proteins that participate in diverse cellular processes. Among the binding partners of DYNLL2, myosin 5a (myo5a) is a motor protein involved in cargo transport. Here we provide a profound characterization of the DYNLL2 binding motif of myo5a in free and DYNLL2 bound form by using NMR spectroscopy, Xray crystallography and molecular dynamics simulations. In the free form the DYNLL2 binding region, located in an intrinsically disordered domain of the myo5a tail, has a nascent helical character. The motif becomes structured and folds into a β-strand upon binding to DYNLL2. Despite all differences of the myo5a sequence from the consensus binding motif, it accommodates into the same DYNLL2 binding groove as all other partners do. Interestingly, while the core motif shows similar interaction pattern in the binding groove as seen inother complexes, the flanking residues make several additional contacts, thereby lengthening the binding motif. The N-terminal extension folds back and partially blocks the free edge of the β-sheet formed by the binding motif itself. The C-terminal extension contacts the dimer interface and interacts with symmetry related residues of the second myo5a peptide. The involvement of flanking residues of the core binding site of myo5a could modify the quaternary structure of the full-length myo5a and affect its biological functions. The presented structural data widen our understanding of the diverse partner recognition of DYNLL proteins and provide an example of a Janus-faced linear motif. 4The LC8 dynein light chains were originally described as the smallest subunit of the microtubuleassociated cytoplasmic dynein motor complex.They show a highly conserved amino acid sequence throughout evolution and they were later shown to bind to more than 70 other proteins involved in various biological processes, therefore they are now considered hub proteins (1, 2).Vertebrates contain two closely related LC8 paralogs, DYNLL1 and DYNLL2 with partially overlapping functions(1). Under physiological conditions LC8proteins arestable homodimers (3).Atomic resolution structureswere determined both for the apo and ligand-bound form using X-ray crystallographyand NMR spectroscopy (4-6). Five β-strands make up two core β-sheets; one sideof each sheet is flanked by two α-helices, and the otherside forms the dimer interface. The β3-strand of one subunit pairs to theβ2"-strandof the other subunitin an antiparallel mode; and the dimer is stabilized by interface contacts through hydrophobic interactions and side chain H-bonds. Two equivalent grooves are formed and they represent the target binding pockets of the dimer. The primary transcript of the human MYO5A geneis processed by alternative splicing (13). Three exons 5 within the tail domain (B, D, and F) are expressed in a cell type-specific manner; the predominant melanocyte-and brain-specific isoforms contains exons D, F, and exon B, respectively (13). The exon pattern of myo5a tail lik...

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DYNLL/LC8: a light chain subunit of the dynein motor complex and beyond

Cited by 132 publications

References 136 publications

Immunogold method evidences that kinesin and myosin bind to and couple microtubules and actin filaments in lipotubuloids of Ornithogalum umbellatum ovary epidermis

Immunogold method evidences that kinesin and myosin bind to and couple microtubules and actin filaments in lipotubuloids of Ornithogalum umbellatum ovary epidermis

A dynein independent role of Tctex-1 at the kinetochore

DYNLL2 Dynein Light Chain Binds to an Extended Linear Motif of Myosin 5a Tail That Has Structural Plasticity

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