Cooperative regulation of C1-domain membrane recruitment polarizes atypical protein kinase C
Recruitment of the Par complex protein atypical protein kinase C (aPKC) to a specific membrane domain is a key step in the polarization of animal cells. While numerous proteins and phospholipids interact with aPKC, how these interactions cooperate to control its membrane recruitment has been unknown...
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| Veröffentlicht in: | The Journal of cell biology 2023-10, Vol.222 (10), p.1 |
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| container_title | The Journal of cell biology |
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| creator | Jones, Kimberly A Drummond, Michael L Penkert, Rhiannon R Prehoda, Kenneth E |
| description | Recruitment of the Par complex protein atypical protein kinase C (aPKC) to a specific membrane domain is a key step in the polarization of animal cells. While numerous proteins and phospholipids interact with aPKC, how these interactions cooperate to control its membrane recruitment has been unknown. Here, we identify aPKC's C1 domain as a phospholipid interaction module that targets aPKC to the membrane of Drosophila neural stem cells (NSCs). The isolated C1 binds the NSC membrane in an unpolarized manner during interphase and mitosis and is uniquely sufficient among aPKC domains for targeting. Other domains, including the catalytic module and those that bind the upstream regulators Par-6 and Bazooka, restrict C1's membrane targeting activity-spatially and temporally-to the apical NSC membrane during mitosis. Our results suggest that aPKC polarity results from cooperative activation of autoinhibited C1-mediated membrane binding activity. |
| doi_str_mv | 10.1083/jcb.202112143 |
| format | Article |
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While numerous proteins and phospholipids interact with aPKC, how these interactions cooperate to control its membrane recruitment has been unknown. Here, we identify aPKC's C1 domain as a phospholipid interaction module that targets aPKC to the membrane of Drosophila neural stem cells (NSCs). The isolated C1 binds the NSC membrane in an unpolarized manner during interphase and mitosis and is uniquely sufficient among aPKC domains for targeting. Other domains, including the catalytic module and those that bind the upstream regulators Par-6 and Bazooka, restrict C1's membrane targeting activity-spatially and temporally-to the apical NSC membrane during mitosis. 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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Cell Membrane Drosophila Kinases Membrane proteins Membranes Mitosis Modules Neural stem cells Neural Stem Cells - metabolism Phospholipids Protein Interaction Domains and Motifs Protein kinase C Protein Kinase C - metabolism Proteins Stem cells |
| title | Cooperative regulation of C1-domain membrane recruitment polarizes atypical protein kinase C |
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