The Mechanism of Dynein Light Chain LC8-mediated Oligomerization of the Ana2 Centriole Duplication Factor

Slevin, Lauren K.; Romes, Erin M.; Dandulakis, M.; Slep, Kevin C.

doi:10.1074/jbc.m114.576041

Cited by 30 publications

(51 citation statements)

References 53 publications

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“…This interaction pair was previously reported from the Drosophila neuroblast asymmetric division (Wang et al , ). Crystallographic studies showed that four LC8 dimers bind to the central region of the Drosophila Ana2/SAS‐5 and that these LC8‐binding sites are not readily apparent in the C. elegans SAS‐5 (Slevin et al , ). Our biochemical data revealed that the interaction between DLC‐1 and SAS‐5 is conserved in C. elegans .…”

Section: Discussionmentioning

confidence: 99%

Centriole translocation and degeneration during ciliogenesis in Caenorhabditis elegans neurons

Zhu

et al. 2017

The EMBO Journal

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Neuronal cilia that are formed at the dendritic endings of sensory neurons are essential for sensory perception. However, it remains unclear how the centriole-derived basal body is positioned to form a template for cilium formation. Using fluorescence time-lapse microscopy, we show that the centriole translocates from the cell body to the dendrite tip in the sensory neurons. The centriolar protein SAS-5 interacts with the dynein light-chain LC8 and conditional mutations of cytoplasmic dynein-1 block centriole translocation and ciliogenesis. The components of the central tube are essential for the biogenesis of centrioles, which later drive ciliogenesis in the dendrite; however, the centriole loses these components at the late stage of centriole translocation and subsequently recruits transition zone and intraflagellar transport proteins. Together, our results provide a comprehensive model of ciliogenesis in sensory neurons and reveal the importance of the dynein-dependent centriole translocation in this process.

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Section: Discussionmentioning

confidence: 99%

Centriole translocation and degeneration during ciliogenesis in Caenorhabditis elegans neurons

Zhu

et al. 2017

The EMBO Journal

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“…In crystal structures of LC8 bound to short linear motifs from several different IDPs [78–80], e.g. Fig.…”

Section: Lc8 Cross-linking Of Idp Duplex Scaffoldsmentioning

confidence: 99%

“…For this, we integrate NMR spectroscopy for study of residue level interactions of flexible domains, X-ray crystallography for atomic level structure of stable complexes, and isothermal titration calorimetry for determination of binding energetics. 13 crystal structures of LC8 bound to peptides have been solved [78–80, 83, 84, 86–90], revealing features of the LC8 recognition motif that confer affinity and specificity. NMR studies of the full-length LC8 binding domain have been performed for multiple binding partners [9, 28], shedding light on the transient structure and dynamics of these regions.…”

Section: Lc8 Cross-linking Of Idp Duplex Scaffoldsmentioning

confidence: 99%

Multivalent IDP assemblies: Unique properties of LC8‐associated, IDP duplex scaffolds

et al. 2015

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A wide variety of subcellular complexes are composed of one or more intrinsically disordered proteins (IDPs) that are multivalent, flexible, and characterized by dynamic binding of diverse partner proteins. These multivalent IDP assemblies, of broad functional diversity, are classified here into five categories distinguished by the number of IDP chains and the arrangement of partner proteins in the functional complex. Examples of each category are summarized in the context of the exceptional molecular and biological properties of IDPs. One type – IDP duplex scaffolds – is considered in detail. Its unique features include parallel alignment of two IDP chains, formation of new self-associated domains, enhanced affinity for additional bivalent ligands, and ubiquitous binding of the hub protein LC8. For two IDP duplex scaffolds, dynein intermediate chain IC and nucleoporin Nup159, these duplex features, together with the inherent flexibility of IDPs, are central to their assembly and function. A new type of IDP-LC8 interaction, distributed binding of LC8 among multiple IDP recognition sites, is described for Nup159 assembly.

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“…Ana2 tetramerizes through the CC and binds Sas6, a rod-shaped protein, through the STAN domain (Stevens et al, 2010a;Shimanovskaya et al, 2013;Dzhindzhev et al, 2014;Slevin et al, 2014;Cottee et al, 2015). Ana2 tetramers may bind and facilitate Sas6 assembly into rings on the mother centriole's surface, ultimately creating the stack of Sas6 rings that form the cartwheel of the nascent procentriole (Stevens et al, 2010b;Guichard et al, 2012;Dzhindzhev et al, 2014;Cottee et al, 2015;Moyer et al, 2015;Rogala et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

An ordered pattern of Ana2 phosphorylation by Plk4 is required for centriole assembly

McLamarrah

Buster

Galletta

et al. 2017

Preprint

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The Mechanism of Dynein Light Chain LC8-mediated Oligomerization of the Ana2 Centriole Duplication Factor

Cited by 30 publications

References 53 publications

Centriole translocation and degeneration during ciliogenesis in Caenorhabditis elegans neurons

Centriole translocation and degeneration during ciliogenesis in Caenorhabditis elegans neurons

Multivalent IDP assemblies: Unique properties of LC8‐associated, IDP duplex scaffolds

An ordered pattern of Ana2 phosphorylation by Plk4 is required for centriole assembly

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