Stable MOB1 interaction with Hippo/MST is not essential for development and tissue growth control

Kulaberoglu, Yavuz; Lin, Kui; Holder, Maxine; Gai, Zhongchao; Gómez, Marta; Shifa, Belul Assefa; Mavis, Merdiye; Hoa, Lily; Sharif, Ahmad A.D.; Lujan, Celia; Smith, Ewan St. John; Bjedov, Ivana; Tapon, Nicolas; Wu, Geng; Hergovich, Alexander

doi:10.1038/s41467-017-00795-y

Cited by 39 publications

(70 citation statements)

References 63 publications

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“…Generally, Mobs are single domain proteins, with an average length of 210-240 amino acids (Hergovich, 2011;Gundogdu and Hergovich, 2019). The Mob/Phocein domain adopts a conserved globular fold, based on solved structures of three classes of Mobs from multiple species: Class I Mobs from Homo sapiens, Xenopus laevis, Mus musculus, and Saccharomyces cerevisiae, a Class II Mob from S. cerevisiae, and a Class IV Mob from H. sapiens (Stavridi et al, 2003;Ponchon et al, 2004;Mrkobrada et al, 2006;Rock et al, 2013;Chung et al, 2014;Gógl et al, 2015;Ni et al, 2015;Kim et al, 2016;Couzens et al, 2017;Kulaberoglu et al, 2017;Xiong et al, 2017;Chen et al, 2018;Parker et al, 2019). This conserved structure is the Mob family fold ( Figure 2B).…”

Section: Shared Structure and Distinguishing Features Between The Foumentioning

confidence: 99%

“…The second distinguishing feature of NDR kinases is the NTR region: a structural domain that functions as the Mobbinding surface (Gógl et al, 2015;Ni et al, 2015;Kim et al, 2016;Kulaberoglu et al, 2017;Parker et al, 2019). Each of the yeast NDR kinases binds to a specific Mob that is necessary, but insufficient, for kinase activity (Komarnitsky et al, 1998;Luca and Winey, 1998a;Frenz et al, 2000;Mah et al, 2001;Colman-Lerner et al, 2001;Hou et al, 2003).…”

Section: Ndr Kinase Domains Involved In Activation and Mob Interactionsmentioning

confidence: 99%

“…the fly Class I Mob, Mats, can physically associate with each of the fly NDR kinases: Warts/LATS and Tricornered (He et al, 2005a). Similarly, mammalian Class I Mobs can bind to either Warts/LATS or Tricornered-like kinases: LATS1/2 and STK38/STK38L, respectively (Bichsel et al, 2004;Devroe et al, 2004;Kohler et al, 2010;Kulaberoglu et al, 2017;Xiong et al, 2017). Partnering dynamics between a Class I Mob and an NDR kinase are conditional and selective, based on structure-function studies of murine and human Class I Mobs bound to the NTR of either a Warts/LATS or Tricornered-like kinase (Ni et al, 2015;Kim et al, 2016;Kulaberoglu et al, 2017).…”

Section: Class I and Ii Mobs Bind Ndr Kinases Through Overlapping Butmentioning

confidence: 99%

“…Phosphorylation of Class I Mobs modulates their binding affinity for different partners (Figure 1). For example, phosphorylation of human Mob1A is necessary for detectable association with the NTR of human LATS1 kinase (Kulaberoglu et al, 2017; see also Praskova et al, 2008;Ni et al, 2015;Kim et al, 2016). In contrast, the NTR of the Tricornered-like kinase, STK38L, will readily bind to an unphosphorylated, N-terminally truncated Mob1A (Mob1A 33−216 ) in isothermal titration calorimetry assays.…”

Section: Class I and Ii Mobs Bind Ndr Kinases Through Overlapping Butmentioning

confidence: 99%

“…The critical amino acids have been identified for formation of mammalian Mob1-NDR kinase complexes (Kohler et al, 2010;Ni et al, 2015;Kim et al, 2016;Kulaberoglu et al, 2017). How specific amino acid contacts contribute to binding specificity was tested for a Class I Mob.…”

Section: Class I and Ii Mobs Bind Ndr Kinases Through Overlapping Butmentioning

confidence: 99%

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Mob Family Proteins: Regulatory Partners in Hippo and Hippo-Like Intracellular Signaling Pathways

Duhart

Raftery

2020

Front. Cell Dev. Biol.

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Studies in yeast first delineated the function of Mob proteins in kinase pathways that regulate cell division and shape; in multicellular eukaryotes Mobs regulate tissue growth and morphogenesis. In animals, Mobs are adaptors in Hippo signaling, an intracellular signal-transduction pathway that restricts growth, impacting the development and homeostasis of animal organs. Central to Hippo signaling are the Nuclear Dbf2-Related (NDR) kinases, Warts and LATS1 and LATS2, in flies and mammals, respectively. A second Hippo-like signaling pathway has been uncovered in animals, which regulates cell and tissue morphogenesis. Central to this emergent pathway are the NDR kinases, Tricornered, STK38, and STK38L. In Hippo signaling, NDR kinase activation is controlled by three activating interactions with a conserved set of proteins. This review focuses on one co-activator family, the highly conserved, non-catalytic Mps1binder-related (Mob) proteins. In this context, Mobs are allosteric activators of NDR kinases and adaptors that contribute to assembly of multiprotein NDR kinase activation complexes. In multicellular eukaryotes, the Mob family has expanded relative to model unicellular yeasts; accumulating evidence points to Mob functional diversification. A striking example comes from the most sequence-divergent class of Mobs, which are components of the highly conserved Striatin Interacting Phosphatase and Kinase (STRIPAK) complex, that antagonizes Hippo signaling. Mobs stand out for their potential to modulate the output from Hippo and Hippo-like kinases, through their roles both in activating NDR kinases and in antagonizing upstream Hippo or Hippo-like kinase activity. These opposing Mob functions suggest that they coordinate the relative activities of the Tricornered/STK38/STK38L and Warts/LATS kinases, and thus have potential to assemble nodes for pathway signaling output. We survey the different facets of Mobdependent regulation of Hippo and Hippo-like signaling and highlight open questions that hinge on unresolved aspects of Mob functions.

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Section: Shared Structure and Distinguishing Features Between The Foumentioning

confidence: 99%

Section: Ndr Kinase Domains Involved In Activation and Mob Interactionsmentioning

confidence: 99%

Section: Class I and Ii Mobs Bind Ndr Kinases Through Overlapping Butmentioning

confidence: 99%

Section: Class I and Ii Mobs Bind Ndr Kinases Through Overlapping Butmentioning

confidence: 99%

Section: Class I and Ii Mobs Bind Ndr Kinases Through Overlapping Butmentioning

confidence: 99%

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Mob Family Proteins: Regulatory Partners in Hippo and Hippo-Like Intracellular Signaling Pathways

Duhart

Raftery

2020

Front. Cell Dev. Biol.

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Varroa destructor parasitism and Deformed wing virus infection in honey bees are linked to peroxisome‐induced pathways

Erban,

Kadleckova,

Sopko

et al. 2024

Proteomics

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The ectoparasitic mite Varroa destructor transmits and triggers viral infections that have deleterious effects on honey bee colonies worldwide. We performed a manipulative experiment in which worker bees collected at emergence were exposed to Varroa for 72 h, and their proteomes were compared with those of untreated control bees. Label‐free quantitative proteomics identified 77 differentially expressed A. mellifera proteins (DEPs). In addition, viral proteins were identified by orthogonal analysis, and most importantly, Deformed wing virus (DWV) was found at high levels/intensity in Varroa‐exposed bees. Pathway enrichment analysis suggested that the main pathways affected included peroxisomal metabolism, cyto‐/exoskeleton reorganization, and cuticular proteins. Detailed examination of individual DEPs revealed that additional changes in DEPs were associated with peroxisomal function. In addition, the proteome data support the importance of TGF‐β signaling in Varroa–DWV interaction and the involvement of the mTORC1 and Hippo pathways. These results suggest that the effect of DWV on bees associated with Varroa feeding results in aberrant autophagy. In particular, autophagy is selectively modulated by peroxisomes, to which the observed proteome changes strongly corresponded. This study complements previous research with different study designs and suggests the importance of the peroxisome, which plays a key role in viral infections.

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MST1/2 Kinase Assays Using Recombinant Proteins

Gómez

Kulaberoglu

Hergovich

2018

Methods in Molecular Biology

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Stable MOB1 interaction with Hippo/MST is not essential for development and tissue growth control

Cited by 39 publications

References 63 publications

Mob Family Proteins: Regulatory Partners in Hippo and Hippo-Like Intracellular Signaling Pathways

Mob Family Proteins: Regulatory Partners in Hippo and Hippo-Like Intracellular Signaling Pathways

Varroa destructor parasitism and Deformed wing virus infection in honey bees are linked to peroxisome‐induced pathways

MST1/2 Kinase Assays Using Recombinant Proteins

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