Collective intracellular cargo transport by multiple kinesins on multiple microtubules

Chen, Kejie; Nam, Woochul; Epureanu, Bogdan I.

doi:10.1103/physreve.101.052413

Cited by 10 publications

(6 citation statements)

References 65 publications

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“…This could be due to numerous reasons such as incomplete depletion of TbKINX1B by RNAi, temporally limited interaction or the requirement of numerous co-factors. Additionally, for each cargo, there may be more than one motor protein, which could indicate functional redundancy as previously described [8,14,43]. Indeed, among the 28 identified T. brucei kinesin genes [44], at least 7 (Tb927.3.2040, Tb927.…”

Section: Tbkinx1b Is a Tbbilbo1 Protein Partnermentioning

confidence: 85%

TbKINX1B: a novel BILBO1 partner and an essential protein in bloodstream form Trypanosoma brucei

et al. 2022

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The flagellar pocket (FP) of the pathogen Trypanosoma brucei is an important single copy structure that is formed by the invagination of the pellicular membrane. It is the unique site of endo- and exocytosis and is required for parasite pathogenicity. The FP consists of distinct structural sub-domains with the least explored being the flagellar pocket collar (FPC). TbBILBO1 is the first-described FPC protein of Trypanosoma brucei. It is essential for parasite survival, FP and FPC biogenesis. In this work, we characterize TbKINX1B, a novel TbBILBO1 partner. We demonstrate that TbKINX1B is located on the basal bodies, the microtubule quartet (a set of four microtubules) and the FPC in T. brucei. Down-regulation of TbKINX1B by RNA interference in bloodstream forms is lethal, inducing an overall disturbance in the endomembrane network. In procyclic forms, the RNAi knockdown of TbKINX1B leads to a minor phenotype with a small number of cells displaying epimastigote-like morphologies, with a misplaced kinetoplast. Our results characterize TbKINX1B as the first putative kinesin to be localized both at the basal bodies and the FPC with a potential role in transporting cargo along with the microtubule quartet.

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Section: Tbkinx1b Is a Tbbilbo1 Protein Partnermentioning

confidence: 85%

TbKINX1B: a novel BILBO1 partner and an essential protein in bloodstream form Trypanosoma brucei

et al. 2022

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“…The head position is defined just by its continuous position along the x-axis, i.e. we do not model the lattice structure of the microtubule unlike in a recent Brownian dynamics model [ 73 ]. We justify this based on the fact that the microtubule has multiple protofilaments and when two kinesins are on different protofilaments they can have same x-position on the microtubule.…”

Section: Methodsmentioning

confidence: 99%

“…We justify this based on the fact that the microtubule has multiple protofilaments and when two kinesins are on different protofilaments they can have same x-position on the microtubule. There are also models that have explicitly incorporated the fact that the motor heads cannot step on each other [ 54 , 73 ], which is likely of more importance when the filament has only a few tracks like actin, which has only two protofilaments in a helix, compared to 10–15 for microtubules.…”

Section: Methodsmentioning

confidence: 99%

Cargo surface fluidity can reduce inter-motor mechanical interference, promote load-sharing and enhance processivity in teams of molecular motors

Sarpangala

Gopinathan

2022

PLoS Comput Biol

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In cells, multiple molecular motors work together as teams to carry cargoes such as vesicles and organelles over long distances to their destinations by stepping along a network of cytoskeletal filaments. How motors that typically mechanically interfere with each other, work together as teams is unclear. Here we explored the possibility that purely physical mechanisms, such as cargo surface fluidity, may potentially enhance teamwork, both at the single motor and cargo level. To explore these mechanisms, we developed a three dimensional simulation of cargo transport along microtubules by teams of kinesin-1 motors. We accounted for cargo membrane fluidity by explicitly simulating the Brownian dynamics of motors on the cargo surface and considered both the load and ATP dependence of single motor functioning. Our simulations show that surface fluidity could lead to the reduction of negative mechanical interference between kinesins and enhanced load sharing thereby increasing the average duration of single motors on the filament. This, along with a cooperative increase in on-rates as more motors bind leads to enhanced collective processivity. At the cargo level, surface fluidity makes more motors available for binding, which can act synergistically with the above effects to further increase transport distances though this effect is significant only at low ATP or high motor density. Additionally, the fluid surface allows for the clustering of motors at a well defined location on the surface relative to the microtubule and the fluid-coupled motors can exert more collective force per motor against loads. Our work on understanding how teamwork arises in cargo-coupled motors allows us to connect single motor properties to overall transport, sheds new light on cellular processes, reconciles existing observations, encourages new experimental validation efforts and can also suggest new ways of improving the transport of artificial cargo powered by motor teams.

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“…This was interpreted to suggest that gE/gI might accelerate KIF1A movement or inhibit opposed dynein-mediated retrograde transport [ 156 ]. However, since gE/gI enhances the efficiency of US9p association with KIF1A [ 152 ] a simpler explanation is that, in the presence of gE/gI, each US9p molecule is more likely to recruit a KIF1A motor to the PRV OEV; larger numbers of attached kinesin motors can result in increased cargo velocities, depending upon the distribution of motors on the cargo surface and the load they encounter [ 157 , 158 ]. Despite the above findings however, evidence for assembly of a gE/gI-US9p-KIF1A complex has been elusive [ 62 , 156 ].…”

Section: Recruitment Of Kinesin Motors To Organelles Transporting Enveloped Virionsmentioning

confidence: 99%

Motor Skills: Recruitment of Kinesins, Myosins and Dynein during Assembly and Egress of Alphaherpesviruses

Wilson

2021

Viruses

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The alphaherpesviruses are pathogens of the mammalian nervous system. Initial infection is commonly at mucosal epithelia, followed by spread to, and establishment of latency in, the peripheral nervous system. During productive infection, viral gene expression, replication of the dsDNA genome, capsid assembly and genome packaging take place in the infected cell nucleus, after which mature nucleocapsids emerge into the cytoplasm. Capsids must then travel to their site of envelopment at cytoplasmic organelles, and enveloped virions need to reach the cell surface for release and spread. Transport at each of these steps requires movement of alphaherpesvirus particles through a crowded and viscous cytoplasm, and for distances ranging from several microns in epithelial cells, to millimeters or even meters during egress from neurons. To solve this challenging problem alphaherpesviruses, and their assembly intermediates, exploit microtubule- and actin-dependent cellular motors. This review focuses upon the mechanisms used by alphaherpesviruses to recruit kinesin, myosin and dynein motors during assembly and egress.

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Collective intracellular cargo transport by multiple kinesins on multiple microtubules

Cited by 10 publications

References 65 publications

TbKINX1B: a novel BILBO1 partner and an essential protein in bloodstream form Trypanosoma brucei

TbKINX1B: a novel BILBO1 partner and an essential protein in bloodstream form Trypanosoma brucei

Cargo surface fluidity can reduce inter-motor mechanical interference, promote load-sharing and enhance processivity in teams of molecular motors

Motor Skills: Recruitment of Kinesins, Myosins and Dynein during Assembly and Egress of Alphaherpesviruses

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