Human FAM154A (SAXO1) is a microtubule-stabilizing protein specific to cilia and related structures

Dacheux, Denis; Roger, Benoît; Bosc, Christophe; Landrein, Nicolas; Roche, Emmanuel; Chansel, Lucie; Trian, Thomas; Andrieux, Annie; Papaxanthos-Roche, Aline; Marthan, Roger; Robinson, Derrick R.; Bonhivers, Mélanie

doi:10.1242/jcs.155143

Cited by 40 publications

(45 citation statements)

References 78 publications

(97 reference statements)

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“…However, it should be noted that our approach has limitations because sometimes, as was the case with STMN2 and STMN3 in jawless fish, organisms would have closer orthologs because of the high similarity of hits or no orthologs would be found because of high dissimilarity of these genes in different taxons. As an example, MAP6 has one ortholog in Danio rerio (Dacheux et al, 2015) which our approach did not show.…”

Section: Increased Numbers Of Orthologs -Mt Skeleton Componentsmentioning

confidence: 60%

The microtubule skeleton and the evolution of neuronal complexity in vertebrates

Trushina

Mulkidjanian

Brandt

2019

Biological Chemistry

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The evolution of a highly developed nervous system is mirrored by the ability of individual neurons to develop increased morphological complexity. As microtubules (MTs) are crucially involved in neuronal development, we tested the hypothesis that the evolution of complexity is driven by an increasing capacity of the MT system for regulated molecular interactions as it may be implemented by a higher number of molecular players and a greater ability of the individual molecules to interact. We performed bioinformatics analysis on different classes of components of the vertebrate neuronal MT cytoskeleton. We show that the number of orthologs of tubulin structure proteins, MT-binding proteins and tubulin-sequestering proteins expanded during vertebrate evolution. We observed that protein diversity of MT-binding and tubulin-sequestering proteins increased by alternative splicing. In addition, we found that regions of the MT-binding protein tau and MAP6 displayed a clear increase in disorder extent during evolution. The data provide evidence that vertebrate evolution is paralleled by gene expansions, changes in alternative splicing and evolution of coding sequences of components of the MT system. The results suggest that in particular evolutionary changes in tubulin-structure proteins, MT-binding proteins and tubulin-sequestering proteins were prominent drivers for the development of increased neuronal complexity.

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Section: Increased Numbers Of Orthologs -Mt Skeleton Componentsmentioning

confidence: 60%

The microtubule skeleton and the evolution of neuronal complexity in vertebrates

Trushina

Mulkidjanian

Brandt

2019

Biological Chemistry

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“…Five mg.mL -1 taxol-stabilised MTs were prepared as in [ 79 ]. For co-sedimentation assays, 4 μL of MTs were mixed with different amounts of protein dialysed in PEMD buffer.…”

Section: Methodsmentioning

confidence: 99%

Interaction between the flagellar pocket collar and the hook complex via a novel microtubule-binding protein in Trypanosoma brucei

et al. 2017

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Trypanosoma brucei belongs to a group of unicellular, flagellated parasites that are responsible for human African trypanosomiasis. An essential aspect of parasite pathogenicity is cytoskeleton remodelling, which occurs during the life cycle of the parasite and is accompanied by major changes in morphology and organelle positioning. The flagellum originates from the basal bodies and exits the cell body through the flagellar pocket (FP) but remains attached to the cell body via the flagellum attachment zone (FAZ). The FP is an invagination of the pellicular membrane and is the sole site for endo- and exocytosis. The FAZ is a large complex of cytoskeletal proteins, plus an intracellular set of four specialised microtubules (MtQ) that elongate from the basal bodies to the anterior end of the cell. At the distal end of the FP, an essential, intracellular, cytoskeletal structure called the flagellar pocket collar (FPC) circumvents the flagellum. Overlapping the FPC is the hook complex (HC) (a sub-structure of the previously named bilobe) that is also essential and is thought to be involved in protein FP entry. BILBO1 is the only functionally characterised FPC protein and is necessary for FPC and FP biogenesis. Here, we used a combination of in vitro and in vivo approaches to identify and characterize a new BILBO1 partner protein—FPC4. We demonstrate that FPC4 localises to the FPC, the HC, and possibly to a proximal portion of the MtQ. We found that the C-terminal domain of FPC4 interacts with the BILBO1 N-terminal domain, and we identified the key amino acids required for this interaction. Interestingly, the FPC4 N-terminal domain was found to bind microtubules. Over-expression studies highlight the role of FPC4 in its association with the FPC, HC and FPC segregation. Our data suggest a tripartite association between the FPC, the HC and the MtQ.

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“…By occupying greater width, a helical structure might influence the spatial organization of the microtubule network (e.g., by inhibiting microtubule co-alignment and bundling), help determine neurite or axonal width, or confer resistance to compressive loads such as might be encountered during development or regeneration (e.g., moving through a glial scar) (34). Given that MAP6 belongs to a family of four genes (MAP6, MAP6D1, FAM154A, and FAM154B) (21,35), understanding the functions of these other proteins could help clarify the special roles of various microtubule types in neurons.…”

Section: Map6 Induces Microtubule Bending: the Frustrated Core-shell mentioning

confidence: 99%

MAP6 is an intraluminal protein that induces neuronal microtubules to coil

et al. 2020

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Neuronal activities depend heavily on microtubules, which shape neuronal processes and transport myriad molecules within them. Although constantly remodeled through growth and shrinkage events, neuronal microtubules must be sufficiently stable to maintain nervous system wiring. This stability is somehow maintained by various microtubule-associated proteins (MAPs), but little is known about how these proteins work. Here, we show that MAP6, previously known to confer cold stability to microtubules, promotes growth. More unexpectedly, MAP6 localizes in the lumen of microtubules, induces the microtubules to coil into a left-handed helix, and forms apertures in the lattice, likely to relieve mechanical stress. These features have not been seen in microtubules before and could play roles in maintaining axonal width or providing flexibility in the face of compressive forces during development.

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Human FAM154A (SAXO1) is a microtubule-stabilizing protein specific to cilia and related structures

Cited by 40 publications

References 78 publications

The microtubule skeleton and the evolution of neuronal complexity in vertebrates

The microtubule skeleton and the evolution of neuronal complexity in vertebrates

Interaction between the flagellar pocket collar and the hook complex via a novel microtubule-binding protein in Trypanosoma brucei

MAP6 is an intraluminal protein that induces neuronal microtubules to coil

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