Interaction of mammalian end binding proteins with CAP-Gly domains of CLIP-170 and p150glued

Bjelić, Saša; Groot, Christian O. De; Schärer, Martin A.; Jaussi, Rolf; Bargsten, Katja; Salzmann, Mara; Frey, Daniel; Capitani, Guido; Kammerer, Richard A.; Steinmetz, Michel O.

doi:10.1016/j.jsb.2011.11.010

Cited by 37 publications

(29 citation statements)

References 35 publications

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“…Dynactin is a 1.1 MDa complex of 11 distinct components that co-precipitates with dynein and is critical for its plus-end targeting and cargo transport functions in vivo (Moughamian et al, 2013; Schroer, 2004; Splinter et al, 2012). p150 contains a CAP-Gly domain that can bind directly to members of the end-binding (EB) protein family such as EB1 or EB3 (Bjelić et al, 2012; Honnappa et al, 2006). EB proteins dynamically track polymerising plus ends through repeated transient binding events on a structure associated with the GTP- or GDP.Pi-tubulin conformation (Akhmanova and Steinmetz, 2015; Bieling et al, 2008, 2007; Maurer et al, 2011, 2012; Zanic et al, 2009; Zhang et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Lissencephaly-1 is a context-dependent regulator of the human dynein complex

Baumbach

Murthy

McClintock

et al. 2017

eLife

126

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The cytoplasmic dynein-1 (dynein) motor plays a central role in microtubule organisation and cargo transport. These functions are spatially regulated by association of dynein and its accessory complex dynactin with dynamic microtubule plus ends. Here, we elucidate in vitro the roles of dynactin, end-binding protein-1 (EB1) and Lissencephaly-1 (LIS1) in the interaction of end tracking and minus end-directed human dynein complexes with these sites. LIS1 promotes dynactin-dependent tracking of dynein on both growing and shrinking plus ends. LIS1 also increases the frequency and velocity of processive dynein movements that are activated by complex formation with dynactin and a cargo adaptor. This stimulatory effect of LIS1 contrasts sharply with its documented ability to inhibit the activity of isolated dyneins. Collectively, our findings shed light on how mammalian dynein complexes associate with dynamic microtubules and help clarify how LIS1 promotes the plus-end localisation and cargo transport functions of dynein in vivo.DOI: http://dx.doi.org/10.7554/eLife.21768.001

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Section: Introductionmentioning

confidence: 99%

Lissencephaly-1 is a context-dependent regulator of the human dynein complex

Baumbach

Murthy

McClintock

et al. 2017

eLife

126

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“…Its plus end-tracking ability depends on both EB1 and CLIP-170 [12]. In vitro assays have demonstrated that p150 glued stabilizes microtubules by associating with EB1 [13].…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of EB1 regulates the recruitment of CLIP-170 and p150glued to the plus ends of astral microtubules

et al. 2016

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Phosphorylation of end-binding protein 1 (EB1), a key member of microtubule plus end-tracking proteins (+TIPs), by apoptosis signal-regulating kinase 1 (ASK1) has been demonstrated to promote the stability of astral microtubules during mitosis by stimulating the binding of EB1 to microtubule plus ends. However, the roles of other members of the +TIPs family in ASK1/EB1-mediated regulation of astral microtubules are unknown. Herein, we show that ASK1-mediated phosphorylation of EB1 enhances the localization of cytoplasmic linker protein 170 (CLIP-170) and p150glued to the plus ends of astral microtubules. Depletion of ASK1 or expression of phospho-deficient or phospho-mimetic EB1 mutants results in changes in the levels of plus-end localized CLIP-170 or p150glued. Mechanistic studies reveal that EB1 phosphorylation promotes its interactions with CLIP-170 and p150glued, thereby recruiting these +TIPs to microtubules. Structural analysis suggests that serine-40 is the primary phosphorylation site on EB1 that exerts these effects. Together, these findings provide novel insight into the molecular mechanisms that regulate the interactions of EB1 with other +TIPs.

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“…This lack of detectable p150 glued interaction with our peptide containing only the last 15 amino-acid residues of EB1 was most likely due to the major contribution of the upstream of EBH domain to the binding of p150 glued CAP-Gly domain to EB1 [6]. This sets the limitations of our affinity probes that may not capture all the CAP-Gly domain-containing proteins in a cell lysate.…”

Section: Discussionmentioning

confidence: 93%

“…Structural characterization of interactions between +TIPs and of +TIPs with microtubules have uncovered a dynamic network [4,5]. EB1 has so far two main sites for interaction with other +TIPs: the hydrophobic cavity/ polar rim in its EBH domain and the acidic C-terminal tail [6]. The EBH domain site interacts with a SxIP motif present in basic and serine-rich sequences of +TIPs such as in the adenomatous polyposis coli (APC) [7].…”

Section: Introductionmentioning

confidence: 99%