JIP1 and JIP3 cooperate to mediate TrkB anterograde axonal transport by activating kinesin-1

Sun, Tao; Li, Yuan; Li, Ting; Ma, Huixian; Guo, Yunyun; Jiang, Xingyu; Hou, Ming; Huang, Shuhong; Chen, Zhe-Yu

doi:10.1007/s00018-017-2568-z

Cited by 32 publications

(40 citation statements)

References 48 publications

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“…At their N-terminal region, both JIP3/4 are composed of leucine zipper segments, the second of which (JIP3 LZ2 ), has also been found to mediate interaction with KLC1 TPR ( Bowman et al, 2000 ; Kelkar et al, 2005 ; Nguyen et al, 2005 ). Functionally, various studies have shown that JIP1 and JIP3 cooperate for kinesin-1-mediated transport ( Hammond et al, 2008 ; Satake et al, 2013 ; Sun et al, 2017 ). To investigate this cooperative effect in the context of our study, we performed co-immunoprecipitation studies ( Figure 5A ).…”

Section: Resultsmentioning

confidence: 99%

“…Interestingly, JIP1 C-term binding to KLC1 TPR is not sufficient to promote kinesin-1 activity ( Kawano et al, 2012 ). Indeed, KHC binding by JIP1 as well as the cooperation of additional proteins, like FEZ1 or JIP3, is required for cargo transport ( Blasius et al, 2007 ; Fu and Holzbaur, 2013 ; Fu and Holzbaur, 2014 ; Hammond et al, 2008 ; Satake et al, 2013 ; Sun et al, 2017 ).…”

Section: Introductionmentioning

confidence: 99%

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Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors

Pernigo

Chegkazi

Yip

et al. 2018

eLife

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The light chains (KLCs) of the heterotetrameric microtubule motor kinesin-1, that bind to cargo adaptor proteins and regulate its activity, have a capacity to recognize short peptides via their tetratricopeptide repeat domains (KLCTPR). Here, using X-ray crystallography, we show how kinesin-1 recognizes a novel class of adaptor motifs that we call ‘Y-acidic’ (tyrosine flanked by acidic residues), in a KLC-isoform specific manner. Binding specificities of Y-acidic motifs (present in JIP1 and in TorsinA) to KLC1TPR are distinct from those utilized for the recognition of W-acidic motifs found in adaptors that are KLC- isoform non-selective. However, a partial overlap on their receptor binding sites implies that adaptors relying on Y-acidic and W-acidic motifs must act independently. We propose a model to explain why these two classes of motifs that bind to the concave surface of KLCTPR with similar low micromolar affinity can exhibit different capacities to promote kinesin-1 activity.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors

Pernigo

Chegkazi

Yip

et al. 2018

eLife

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“…Various studies have shown that JIP1 and JIP3 act co-operatively in kinesin-1-mediated transport (Hammond et al, 2008;Satake et al, 2013;Sun et al, 2017). Like JIP1, JIP3 belongs to the JIP family of adaptor proteins that in mammals is composed of four members (Whitmarsh, 2006).…”

Section: Jip1 C-term Loading Does Not Affect the Affinity Of Jip3 Lz2mentioning

confidence: 99%

“…Interestingly, JIP1 C-term binding to KLC1 TPR is not sufficient to promote kinesin-1 activity (Kawano et al, 2012). Indeed, KHC binding by JIP1 as well as the cooperation of additional proteins, like FEZ1 or JIP3, is required for cargo transport (Blasius et al, 2007;Holzbaur, 2013, 2014;Hammond et al, 2008;Satake et al, 2013;Sun et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors

Pernigo¹,

Chegkazi

Yip

et al. 2018

Preprint

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The light chains (KLCs) of the heterotetrameric microtubule motor kinesin-1, that bind to cargo adaptor proteins and regulate its activity, have a capacity to recognize short peptides via their tetratricopeptide repeat domains (KLC TPR ). Here, using X-ray crystallography, we show how kinesin-1 recognizes a novel class of adaptor motifs that we call 'Y-acidic' (tyrosine flanked by acidic residues), in a KLC-isoform specific manner. Binding specificities of Y-acidic motifs (present in JIP1 and in TorsinA) to KLC1 TPR are distinct from those utilized for the recognition of W-acidic motifs found in adaptors that are KLCisoform non-selective. However, a partial overlap on their receptor binding sites implies that adaptors relying on Y-acidic and W-acidic motifs must act independently. We propose a model to explain why these two classes of motifs that bind to the concave surface of KLC TPR with similar low micromolar affinity can exhibit different capacities to promote kinesin-1 activity.(147 words) 3

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“…Sunday Driver (Syd) or JNK-interacting protein-3 (JIP3) belongs to a family of conserved scaffolding proteins that bind to and facilitate JNK activation (Davis and Tapon, 2019;Davis, 2000;Kelkar et al, 2000). Syd/JIP3 also regulates vesicle transport in worm and mammalian cells (Caswell and Dickens, 2018;Choudhary et al, 2017;Edwards et al, 2013;Gowrishankar et al, 2017;Sun et al, 2017;Taylor and Alessi, 2020).…”

Section: Introductionmentioning

confidence: 99%

Syd/JIP3 Controls Tissue Size by Regulating Diap1 Protein Turnover Downstream of Yorkie/YAP

Ahmad

Vadla

Chabu

2020

Preprint

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Highlights• Syd/JIP3 is required for proper Drosophila wing size• Syd/JIP3 functions downstream of Yorkie by stabilizing Diap1 to promote cell survival during rapid tissue growth • Yorkie-mediated tissue growth is highly sensitive to Syd/JIP3 dosage • Syd/JIP3 is downregulated at the end of the tissue expansion phase AbstractHow organisms control organ size is not fully understood. We found that Syd/JIP3 is required for proper wing size in Drosophila. JIP3 mutations are associated with organ size defects in mammals.Our mechanistic studies place Syd/JIP3 downstream of Hippo. Syd/JIP3 is dispensable for Hippo transcriptional activity but it is essential for Diap1 protein stability and function. Consistent with this observation, Syd/JIP3 inhibition reduces Diap1 protein levels and, correspondingly, elevates cell death in wing tissues. Partial restoration of Diap1 rescues wing size. In addition, Syd/JIP3 is upregulated in response to Yorkie activation. Importantly, Syd/JIP3 is required for the full effect of Yorkie-mediated tissue overgrowth. Thus, Syd/JIP3 is a novel organ size regulator in the Hippo pathway. This study provides mechanistic insights into the recent and perplexing link between JIP3 mutations and organ size defects in mammals, including in humans where de novo JIP3 variants are associated with microcephaly.

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JIP1 and JIP3 cooperate to mediate TrkB anterograde axonal transport by activating kinesin-1

Cited by 32 publications

References 48 publications

Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors

Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors

Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors

Syd/JIP3 Controls Tissue Size by Regulating Diap1 Protein Turnover Downstream of Yorkie/YAP

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