Spastin-Interacting Protein NA14/SSNA1 Functions in Cytokinesis and Axon Development

Goyal, Uma; Renvoisé, Benoît; Chang, Jaerak; Blackstone, Craig

doi:10.1371/journal.pone.0112428

Cited by 22 publications

(32 citation statements)

References 50 publications

(69 reference statements)

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“…and ). As previously reported, spastin exists in two major isoforms (spastin M1 and spastin M87 ) based on different translation initiation sites at residues 1 or 87 (Solowska et al .,), and spastin M87 is highly expressed in the neural tissue (Goyal et al ., ). We demonstrated that exogenous spastin protein exists in the cytoplasm as particles, which is consistent with a previous report (Roll‐Mecak and Vale, ; Finsterer et al ., ), and that spastin colocalizes with CRMP5 in the neurites and the cell bodies of neurons (Figs.…”

Section: Discussionmentioning

confidence: 97%

Spastin Interacts with CRMP5 to Promote Neurite Outgrowth by Controlling the Microtubule Dynamics

Zhang²,

Chen

et al. 2018

Developmental Neurobiology

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Changing the microtubule dynamics is sufficient to alter the axon and dendrite specification and development. Spastin participates in the growth and regeneration of neurites by severing microtubules into small segments, and collapsin response mediator protein 5 (CRMP5) provides structural support and serves as a track for cargo transport by promoting microtubule polymerization. Nevertheless, how spastin and CRMP5 cooperate to regulate neurite outgrowth by controlling the microtubule dynamics needs to be elucidated. In our present study, spastin interacted with CRMP5 in vitro and in vivo. The binding domains for the spastin and CRMP5 interaction were the N‐terminal fragment of spastin (residues 270–328) and the C‐terminal fragment of CRMP5 (residues 472–564). Spastin and its truncation mutants, including the microtubule‐binding domain (MTBD) and ATPases associated with diverse cellular activities (AAA) domain, were necessary for the severing of microtubules. Furthermore, we demonstrated that microtubule polymerization of CRMP5 interfered with the microtubule‐severing function of spastin. Knocking down either spastin or CRMP5 inhibited neurite outgrowth in hippocampal neurons. However, co‐transfected spastin and CRMP5 promoted the outgrowth of neurites including dendrites and axons. Taken together, our data support a model in which the spastin interaction with CRMP5 promotes neurite outgrowth by controlling the microtubule dynamics.

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Section: Discussionmentioning

confidence: 97%

Spastin Interacts with CRMP5 to Promote Neurite Outgrowth by Controlling the Microtubule Dynamics

Zhang²,

Chen

et al. 2018

Developmental Neurobiology

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“…SCOC was recently identified as a positive regulator of starvation-induced autophagy (58,59), presumably via its interaction with FEZ1 (fasciculation and elongation protein zeta 1), an inhibitor of the autophagy induction. SSNA1 is a putative coiled-coil protein and is involved in regulating cell division and cytokinesis as well as adult axonal development, presumably by interacting and modulating spastin, a microtubule-severing AAA ATPase (60). SCOC and SNNA1 were determined to interact with the 26S proteasome directly through a single cross-link with the coiled-coil region of Rpt6 respectively, i.e.…”

Section: Fig 5 Classification Of Human 26s Proteasomes Reveals Varimentioning

confidence: 99%

Molecular Details Underlying Dynamic Structures and Regulation of the Human 26S Proteasome

Wang

Cimermančič

et al. 2017

Molecular & Cellular Proteomics

118

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The 26S proteasome is the macromolecular machine responsible for ATP/ubiquitin dependent degradation. As aberration in proteasomal degradation has been implicated in many human diseases, structural analysis of the human 26S proteasome complex is essential to advance our understanding of its action and regulation mechanisms. In recent years, cross-linking mass spectrometry (XL-MS) has emerged as a powerful tool for elucidating structural topologies of large protein assemblies, with its unique capability of studying protein complexes in cells. To facilitate the identification of cross-linked peptides, we have previously developed a robust amine reactive sulfoxide-containing MS-cleavable cross-linker, disuccinimidyl sulfoxide (DSSO). To better understand the structure and regulation of the human 26S proteasome, we have established new DSSO-based and XL-MS workflows by coupling with HB-tag based affinity purification to comprehensively examine protein-protein interactions within the 26S proteasome. In total, we have identified 447 unique lysine-to-lysine linkages delineating 67 interprotein and 26 intraprotein interactions, representing the largest cross-link dataset for proteasome complexes. In combination with EM maps and computational modeling, the architecture of the 26S proteasome was determined to infer its structural dynamics. In particular, three proteasome subunits Rpn1, Rpn6, and Rpt6 displayed multiple conformations that have not been previously reported. Additionally, cross-links between proteasome subunits and 15 proteasome interacting proteins including 9 known and 6 novel ones have been determined to demonstrate their physical interactions at the amino acid level. Our results have provided new insights on the dynamics of the 26S human proteasome and the methodologies presented here can be applied to study other protein complexes.

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“…RNA-mediated knockdown of DIP13 resulted in a phenotype of multiflagellated and multinucleated cells, suggesting a cytokinesis defect. The mammalian DIP13 homolog, NA14, is a centrosomal protein the knockdown phenotype of which also results in cytokinesis defects (Goyal et al, 2014). The specific relationship between DIP13/NA14 and centrosomal function remains to be determined.…”

Section: Mutants That Affect the Spatial Coordination Of Cell Divisionmentioning

confidence: 99%

The Chlamydomonas cell cycle

2015

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SummaryThe position of Chlamydomonas within the eukaryotic phylogeny makes it a unique model in at least two important ways: as a representative of the critically important, early‐diverging lineage leading to plants; and as a microbe retaining important features of the last eukaryotic common ancestor (LECA) that has been lost in the highly studied yeast lineages. Its cell biology has been studied for many decades and it has well‐developed experimental genetic tools, both classical (Mendelian) and molecular. Unlike land plants, it is a haploid with very few gene duplicates, making it ideal for loss‐of‐function genetic studies. The Chlamydomonas cell cycle has a striking temporal and functional separation between cell growth and rapid cell division, probably connected to the interplay between diurnal cycles that drive photosynthetic cell growth and the cell division cycle; it also exhibits a highly choreographed interaction between the cell cycle and its centriole–basal body–flagellar cycle. Here, we review the current status of studies of the Chlamydomonas cell cycle. We begin with an overview of cell‐cycle control in the well‐studied yeast and animal systems, which has yielded a canonical, well‐supported model. We discuss briefly what is known about similarities and differences in plant cell‐cycle control, compared with this model. We next review the cytology and cell biology of the multiple‐fission cell cycle of Chlamydomonas. Lastly, we review recent genetic approaches and insights into Chlamydomonas cell‐cycle regulation that have been enabled by a new generation of genomics‐based tools.

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Spastin-Interacting Protein NA14/SSNA1 Functions in Cytokinesis and Axon Development

Cited by 22 publications

References 50 publications

Spastin Interacts with CRMP5 to Promote Neurite Outgrowth by Controlling the Microtubule Dynamics

Spastin Interacts with CRMP5 to Promote Neurite Outgrowth by Controlling the Microtubule Dynamics

Molecular Details Underlying Dynamic Structures and Regulation of the Human 26S Proteasome

The Chlamydomonas cell cycle

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