Apical Complex Genes Control Mitotic Spindle Geometry and Relative Size of Daughter Cells in Drosophila Neuroblast and pI Asymmetric Divisions

Cai, Yu; Yu, Fengwei; Lin, Shuping; Chia, William; Yang, Xiaohang

doi:10.1016/s0092-8674(02)01170-4

Cited by 131 publications

(138 citation statements)

References 42 publications

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“…These disturbances of junctional complexes are presumed to lead to the denudation of the apical epithelium 18 . In flies and worms, the apical complex proteins help localize cell fate determinants, such as Numb and Miranda, but there are redundant mechanisms for Numb localization 19,20 .…”

Section: Nature Genetics Volume 36 | Number 3 | March 2004 267mentioning

confidence: 99%

The hyh mutation uncovers roles for αSnap in apical protein localization and control of neural cell fate

et al. 2004

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The hyh (hydrocephalus with hop gait) mouse shows a markedly small cerebral cortex at birth and dies postnatally from progressive enlargement of the ventricular system 1,2 . Here we show that the small hyh cortex reflects altered cell fate. Neural progenitor cells withdraw prematurely from the cell cycle, producing more early-born, deep-layer cerebral cortical neurons but depleting the cortical progenitor pool, such that late-born, upper-layer cortical neurons are underproduced, creating a small cortex. hyh mice carry a hypomorphic missense mutation in the gene Napa encoding soluble N-ethylmaleimidesensitive factor (NSF) attachment protein alpha (αSnap), involved in SNAP receptor (SNARE)-mediated vesicle fusion in many cellular contexts. A targeted null Napa mutation is embryonically lethal. Altered neural cell fate is accompanied by abnormal localization of many apical proteins implicated in regulation of neural cell fate, including E-cadherin, β-catenin, atypical protein kinase C (aPKC) and INADL (inactivation-noafterpotential D-like, also known as protein associated with Lin7, or Pals1). Apical localization of the SNARE Vamp7 is also disrupted. Thus, αSnap is essential for apical protein localization and cell fate determination in neuroepithelial cells.

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Section: Nature Genetics Volume 36 | Number 3 | March 2004 267mentioning

confidence: 99%

The hyh mutation uncovers roles for αSnap in apical protein localization and control of neural cell fate

et al. 2004

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“…Par-3 can regulate the Rho-family GTPases through GEFs (guanine nucleotide exchange factors) to mediate actin reorganization and possibly control axonal sorting and the unidirectional ensheathment of the axon (Benninger et al, 2007;Bryan and D'Amore, 2007;Nodari et al, 2007). Additionally, during asymmetric cell division, Par-3 recruits proteins such as Inscuteable, which in turn recruits Partner of Inscuteable (Pins) (Cai et al, 2003;Siller et al, 2006). Pins directly associates with heterotrimeric G-protein subunits and microtubuleassociated proteins to dictate the orientation of the microtubules and their positioning along the cell cortex (Izumi et al, 2006;Siller et al, 2006;Morin et al, 2007;Konno et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

Assessing the Role of the Cadherin/Catenin Complex at the Schwann Cell–Axon Interface and in the Initiation of Myelination

Lewallen¹,

Shen²,

Torre³

et al. 2011

J. Neurosci.

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Myelination is dependent on complex reciprocal interactions between the Schwann cell (SC) and axon. Recent evidence suggests that the SC-axon interface represents a membrane specialization essential for myelination; however, the manner in which this polarized-apical domain is generated remains a mystery. The cell adhesion molecule N-cadherin is enriched at the SC-axon interface and colocalizes with the polarity protein Par-3. The asymmetric localization is induced on SC-SC and SC-axon contact. Knockdown of N-cadherin in SCs cocultured with DRG neurons disrupts Par-3 localization and delays the initiation of myelination. However, knockdown or overexpression of neuronal N-cadherin does not influence the distribution of Par-3 or myelination, suggesting that homotypic interactions between SC and axonal N-cadherin are not essential for the events surrounding myelination. To further investigate the role of N-cadherin, mice displaying SC-specific gene ablation of N-cadherin were generated and characterized. Surprisingly, myelination is only slightly delayed, and mice are viable without any detectable myelination defects. ␤-Catenin, a downstream effector of N-cadherin, colocalizes and coimmunoprecipitates with N-cadherin on the initiation of myelination. To determine whether ␤-catenin mediates compensation on N-cadherin deletion, SC-specific gene ablation of ␤-catenin was generated and characterized. Consistent with our hypothesis, myelination is more severely delayed than when manipulating N-cadherin alone, but without any defect to the myelin sheath. Together, our results suggest that N-cadherin interacts with ␤-catenin in establishing SC polarity and the timely initiation of myelination, but they are nonessential components for the formation and maturation of the myelin sheath.

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“…Par6 was initially identified as a product of par-6, one of the par genes, which is essential for asymmetric cell division in the early embryo of Caenorhabditis elegans (20). The aPKC-Par6 complex is conserved from nematodes to mammals as a cell polarity regulator (5,21) and is involved in various cell polarity-related processes, such as asymmetric cell division (22,23), directed cell migration (24,25), axon specification (26), and tight junction formation (27)(28)(29)(30)(31), wherein the aPKC-Par6 complex shows a specific localization in each signaling process. A defect in PB1-PB1 interaction between aPKC and Par6 results in incomplete localization (32).…”

mentioning

confidence: 99%

Solution Structure of Atypical Protein Kinase C PB1 Domain and Its Mode of Interaction with ZIP/p62 and MEK5

Hirano

Yoshinaga

Ogura

et al. 2004

Journal of Biological Chemistry

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Atypical protein kinase C (aPKC) has been implicated in several signaling pathways such as cell polarity, cell survival, and cell differentiation. In contrast to other PKCs, aPKC is unique in having the PB1 (Phox and Bem 1) domain in the N terminus. The aPKC PB1 domain binds with ZIP/p62, Par6, or MEK5 through a PB1-PB1 domain interaction that controls the localization of aPKC. Here, we determined the three-dimensional structure of the PB1 domain of PKC by NMR and found that the PB1 domain adopts a ubiquitin fold. The OPCA (OPR, PC, and AID) motif inserted into the ubiquitin fold was presented as a ␤␤␣ fold in which the side chains of conserved Asp residues were oriented to the same direction to form an acidic surface. This structural feature suggested that the acidic surface of the PKC PB1 domain interacted with the basic surface of the target PB1 domains, and this was confirmed in the case of the PKC -ZIP/p62 complex by mutational analysis. Interestingly, in the PKC PB1 domain a conserved lysine residue was located on the side opposite to the OPCA motifpresenting surface, suggesting dual roles for the PKC PB1 domain in that it could interact with either the conserved lysine residue or the acidic residues on the OPCA motif of the target PB1 domains.As part of the ongoing study of atypical protein kinase C (aPKC), 1 isoform PKC was first cloned in 1988 (1), followed by the cloning of isoform PKC / (2, 3). Now, aPKC has been suggested as playing a crucial role in signal transduction pathways such as cell polarity, cell differentiation, and cell survival (4, 5). In contrast to conventional PKC, aPKC contains only a single C1 domain but is devoid of a C2 domain in the Nterminal regulatory region. A tandem repeat of the C1 domain is known to be a target of diacylglycerol, and the C2 domain is a binding site for Ca 2ϩ . However, because of the lack of a C2 domain and the incomplete C1 domain in aPKC, neither Ca 2ϩ nor diacylglycerol activates aPKC. Instead, aPKC contains a PB1 domain at the N terminus.In PKC signaling, the regulation of both the catalytic activity and the spatial localization of PKC is essential. PKC is known to translocate to a specific region in response to activation signals and then phosphorylate specific target proteins. Such spatial localization of PKC in cells is partially regulated by either PKC-binding scaffold proteins or anchoring proteins (6). In particular, aPKC binds with PB1 domain-containing proteins such as ZIP/p62 (7-9), Par6 (10 -13), or MEK5 (14) through the PB1-PB1 domain interaction. Thus, the PB1-mediated interaction between aPKC and the scaffolding or anchoring proteins plays a crucial role in exerting the biological functions of aPKC (4).ZIP/p62 homologues were isolated in different biological contexts as ZIP, p62, and EBIAP (7,15,16). Recently, it has been demonstrated that ZIP/p62 is involved in the NF B activation pathway in association with aPKC. ZIP/p62 is a scaffold protein of aPKC for the activation of NF B downstream of extracellular signals such as tumor necrosis fac...

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Apical Complex Genes Control Mitotic Spindle Geometry and Relative Size of Daughter Cells in Drosophila Neuroblast and pI Asymmetric Divisions

Cited by 131 publications

References 42 publications

The hyh mutation uncovers roles for αSnap in apical protein localization and control of neural cell fate

The hyh mutation uncovers roles for αSnap in apical protein localization and control of neural cell fate

Assessing the Role of the Cadherin/Catenin Complex at the Schwann Cell–Axon Interface and in the Initiation of Myelination

Solution Structure of Atypical Protein Kinase C PB1 Domain and Its Mode of Interaction with ZIP/p62 and MEK5

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