2018
DOI: 10.1038/s41589-018-0117-1
|View full text |Cite
|
Sign up to set email alerts
|

Establishment of the PAR-1 cortical gradient by the aPKC-PRBH circuit

Abstract: Cell polarity is the asymmetric compartmentalization of cellular components. An opposing gradient of partitioning-defective protein kinases, atypical protein kinase C (aPKC) and PAR-1, at the cell cortex guides diverse asymmetries in the structure of metazoan cells, but the mechanism underlying their spatial patterning remains poorly understood. Here, we show in Caenorhabditis elegans zygotes that the cortical PAR-1 gradient is patterned as a consequence of dual mechanisms: stabilization of cortical dynamics a… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
33
0

Year Published

2019
2019
2022
2022

Publication Types

Select...
5
3

Relationship

0
8

Authors

Journals

citations
Cited by 25 publications
(34 citation statements)
references
References 55 publications
1
33
0
Order By: Relevance
“…By analogy, binding with Scrib and/or Dlg could allosterically regulate Lgl to prevent phosphorylation, although we have ruled out Lgl-Scrib and Lgl-Dlg interactions documented in the literature (34,66). Scrib or Dlg might also act as a "decoy substrate" for aPKC, as PAR-2 does in PAR-1 protection (63). Indeed, Scrib is phosphorylated on at least 13 residues in Drosophila embryos, though the functional relevance of this is not yet known (67).…”
Section: Discussionmentioning
confidence: 98%
“…By analogy, binding with Scrib and/or Dlg could allosterically regulate Lgl to prevent phosphorylation, although we have ruled out Lgl-Scrib and Lgl-Dlg interactions documented in the literature (34,66). Scrib or Dlg might also act as a "decoy substrate" for aPKC, as PAR-2 does in PAR-1 protection (63). Indeed, Scrib is phosphorylated on at least 13 residues in Drosophila embryos, though the functional relevance of this is not yet known (67).…”
Section: Discussionmentioning
confidence: 98%
“…LGL-1/Lgl and PAR-1. Both proteins are direct aPKC targets in epithelia, and in the C. elegans zygote their anterior exclusion is mediated by PKC-3 (Beatty et al, 2010;Betschinger et al, 2003;Doerflinger et al, 2010;Hoege et al, 2010;Hurov et al, 2004;Motegi et al, 2011;Plant et al, 2003;Ramanujam et al, 2018;Yamanaka et al, 2003). For these experiments we made use of integrated LGL-1::GFP transgene (Waaijers et al, 2015) and an endogenously tagged PAR-1::GFP fusion.…”
Section: Par-6 and Pkc-3 Mediate Apical Lgl-1 Exclusion And Promote Jmentioning
confidence: 99%
“…Regulated binding of plasma membrane lipids has emerged as a common theme. The polarity-related proteins Par1, Lgl, Miranda, Numb, PAR-2 and the anterior protein Par3 share a common ability to bind anionic phospholipids, most likely the plasma membrane-enriched PIP2, via dedicated domains [31][32][33][34][35][36]. A shared characteristic of numerous polarity-related proteins, these domains are often the direct targets of regulatory kinases, allowing membrane association to be regulated in time and space.…”
Section: Local Retentionmentioning
confidence: 99%
“…Instead, molecules typically engage in multivalent association with the membrane through the formation of homo-or hetero-dimeric complexes (Figure 2A). PAR-2 and Par3 form homo-oligomers [30,38], while PAR-1 and the related MARK kinases are thought to require coincident binding to plasma membrane lipids along with additional accessory factors, such as the C. elegans PAR-2 protein, to achieve maximal membrane enrichment [31]. In the case of Par3, it is precisely these higher-order, multivalent interactions that allow formation of stable, slow-diffusing, membrane-associated clusters that are segregated by cortical flows as discussed above and which likely play a role in numerous systems [38,39].…”
Section: Local Retentionmentioning
confidence: 99%