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SosaLab @SosaLab4

Structure & function of biological molecular machines

Joined May 2020
  • Tweets 12
  • Following 42
  • Followers 68
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SosaLab@SosaLab4
2 Jul 2024
nature.com/articles/s41467-0…

Cryo-EM unveils kinesin KIF1A’s processivity mechanism and the impact of its pathogenic variant...

Nature Communications - Benoit et al. present high-resolution structures of dimeric microtubule-bound KIF1A, including its pathogenic P305L mutant. Their findings provide insights into...

nature.com
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SosaLab@SosaLab4
31 Aug 2023
New insights into the mechanochemical coupling mechanism of kinesin–microtubule complexes from their high-resolution structures doi.org/10.1042/BST20221238
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SosaLab retweeted
Luke Rosen
@lukebrosen
3 Feb 2023
Congrats @arnegennerich and all, this is a huge breakthrough to have such detailed structures of KIF1A bound to microtubules! Very important work. Thank you from all our families and the whole community.
Arne
@arnegennerich
3 Feb 2023
The Sosa and Gennerich Labs report the fist near-atomic structures of KIF1A bound to microtubules. biorxiv.org/content/10.1101/…
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SosaLab@SosaLab4
3 Feb 2023
High-Resolution structures of microtubule-bound KIF1A and its pathogenic variant P305L biorxiv.org/content/10.1101/…

High-Resolution structures of microtubule-bound KIF1A and its pathogenic variant P305L

Mutations in the Kinesin-3 motor KIF1A, a microtubule (MT)-associated motor protein, cause devastating neurodevelopmental and neurodegenerative diseases termed KIF1A-associated neurological disorders...

biorxiv.org
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SosaLab@SosaLab4
20 Dec 2022
Nucleotide-free structures of Kif20A illuminate the atypical allostery in this mitotic kinesin-6 biorxiv.org/content/10.1101/…

Nucleotide-free structures of Kif20A illuminate the atypical allostery in this mitotic kinesin-6

KIF20A is a critical kinesin for cell division and a promising anti-cancer drug target. The mechanisms underlying its cellular roles remain elusive. Interestingly, unusual coupling between the...

biorxiv.org
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SosaLab@SosaLab4
27 Jul 2022
Our recent work in collaboration with the Allingham's lab describing the mechanism of combined motile and depolymerization activities by a kinesin-8 just came out! nature.com/articles/s41467-0…

Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin...

Nature Communications - Kinesin-8s are dual-activity motor proteins that can move processively on microtubules and depolymerize microtubule plus-ends. This study shows how kinesin-8s alternate...

nature.com
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SosaLab@SosaLab4
7 Mar 2022
Our latest preprint on the Kinesin-8 combined motile & microtubule depolymerization mechanism dlvr.it/SKrQYT
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SosaLab@SosaLab4
17 Jun 2021
nature.com/articles/s41467-0… Just out! Significant additions to the preprint biorxiv.org/cgi/content/shor… are the separation of coexisting motor-head conformations and improved resolution (2.7-3.9 Å now). @matthieuBenoit1 @HernandoSosa4 @SEMC_NYSBC @cryoEM_Papers #microtubule #kinesin
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SosaLab@SosaLab4
17 Jun 2021
nature.com/articles/s41467-0…
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SosaLab@SosaLab4
4 Jun 2020
Glad to see our paper finally coming out with 18 cryo-EM snapshosts of the molecular motor KIF14. biorxiv.org/content/10.1101/…

Structural basis of mechano-chemical coupling by the mitotic kinesin KIF14

KIF14 is a mitotic kinesin protein important for cytokinesis. Its overexpression is associated with a variety of cancers and mutations in KIF14 result in cerebral and renal development defects. Like...

biorxiv.org
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SosaLab retweeted
Matthieu Benoit@matthieuBenoit1
3 Jun 2020
18 new #cryoEM structures of the kinesin molecular motor KIF14 reveal its translocation mechanism @SosaLab4 biorxiv.org/cgi/content/shor… Collaboration with Kwok lab. Data collected at @SEMC_NYSBC #EinsteinMed #MTmotors #kinesins #microtubules #biophysics @cryoEM_Papers #cellbiology
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SosaLab retweeted
Nature Communications@NatureComms
27 Apr 2018
Sosa lab @EinsteinMed provides structural insights into kinesin-13 mediated microtubule depolymerisation. go.nature.com/2HQuXoi
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