2018
DOI: 10.7554/elife.36374
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MAP7 regulates axon morphogenesis by recruiting kinesin-1 to microtubules and modulating organelle transport

Abstract: Neuronal cell morphogenesis depends on proper regulation of microtubule-based transport, but the underlying mechanisms are not well understood. Here, we report our study of MAP7, a unique microtubule-associated protein that interacts with both microtubules and the motor protein kinesin-1. Structure-function analysis in rat embryonic sensory neurons shows that the kinesin-1 interacting domain in MAP7 is required for axon and branch growth but not for branch formation. Also, two unique microtubule binding sites … Show more

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Cited by 61 publications
(88 citation statements)
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“…The modification could either directly affect the efficiency of the molecular motors, such as kinesins and dynein (Ikegami et al, 2007;Sirajuddin et al, 2014), or alternatively affect the microtubule binding of other proteins that affect cargo transport (Kang et al, 2008;Barlan et al, 2013;Semenova et al, 2014;Monroy et al, 2018;Tymanskyj et al, 2018). How polyglutamylation regulates the transport of distinct axonal cargoes needs to be determined.…”
Section: Of 14mentioning
confidence: 99%
“…The modification could either directly affect the efficiency of the molecular motors, such as kinesins and dynein (Ikegami et al, 2007;Sirajuddin et al, 2014), or alternatively affect the microtubule binding of other proteins that affect cargo transport (Kang et al, 2008;Barlan et al, 2013;Semenova et al, 2014;Monroy et al, 2018;Tymanskyj et al, 2018). How polyglutamylation regulates the transport of distinct axonal cargoes needs to be determined.…”
Section: Of 14mentioning
confidence: 99%
“…S2A) are largely unchanged in the presence of MAP7. MAP7 binds to kinesin-1 on the stalk domain, near the hinge region that mediates auto-inhibition (19,23,28). Thus, we asked if MAP7 acts both to recruit kinesin-1 to microtubules and relieve auto-inhibition (29,30).…”
Section: Resultsmentioning
confidence: 99%
“…To assess the possibility of an interaction between MAP7 and kinesin-2, we performed a global alignment of kinesin-1 (Heavy Chain) and kinesin-2 motors as MAP7 interacts with the stalk domain of the kinesin-1 heavy chain ( Fig. S4A) (19). We observe no homology in the kinesin-1 and kinesin-2 stalk domains, indicating that MAP7 is unlikely to directly interact with kinesin-2.…”
Section: Map7 Regulates Bidirectional Transport By Tuning the Kinesinmentioning
confidence: 99%
See 1 more Smart Citation
“…For example, tau and MAP2 proteins both inhibit kinesin-1 motility (Heins et al, 1991;Seitz et al, 2002;Vershinin et al, 2007;Dixit et al, 2008). In contrast, MAP7 recruits kinesin-1 to microtubules and activates motility (Barlan et al, 2013;Tymanskyj et al, 2018;Chaudhary et al, 2019;Hooikaas et al, 2019).…”
Section: Discussionmentioning
confidence: 99%