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- aggregation classification "A1".
- aggregation creator B439405.
- aggregation creator B439406.
- aggregation creator B439407.
- aggregation creator B439408.
- aggregation creator B439409.
- aggregation creator B439410.
- aggregation creator B439411.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2011".
- aggregation format "application/pdf".
- aggregation hasFormat 1854252.bibtex.
- aggregation hasFormat 1854252.csv.
- aggregation hasFormat 1854252.dc.
- aggregation hasFormat 1854252.didl.
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- aggregation isPartOf urn:issn:1001-0602.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Phosphorylation switch modulates the interdigitated pattern of PIN1 localization and cell expansion in Arabidopsis leaf epidermis".
- aggregation abstract "Within a multicellular tissue cells may coordinately form a singular or multiple polar axes, but it is unclear whether a common mechanism governs different types of polar axis formation. The phosphorylation status of PIN proteins, which is directly affected by the PINOID (PID) protein kinase and the PP2A protein phosphatase, is known to regulate the apical-basal polarity of PIN localization in bipolar cells of roots and shoot apices. Here, we provide evidence that the phosphorylation status-mediated PIN polarity switch is widely used to modulate cellular processes in Arabidopsis including multipolar pavement cells (PC) with interdigitated lobes and indentations. The degree of PC interdigitation was greatly reduced either when the FYPP1 gene, which encodes a PP2A called phytochrome-associated serine/threonine protein phosphatase, was knocked out or when the PID gene was overexpressed (35S::PID). These genetic modifications caused PIN1 localization to switch from lobe to indentation regions. The PP2A and PID mediated switching of PIN1 localization is strikingly similar to their regulation of the apical-basal polarity switch of PIN proteins in other cells. Our findings suggest a common mechanism for the regulation of PIN1 polarity formation, a fundamental cellular process that is crucial for pattern formation both at the tissue/organ and cellular levels.".
- aggregation authorList BK766758.
- aggregation endPage "978".
- aggregation issue "6".
- aggregation startPage "970".
- aggregation volume "21".
- aggregation aggregates 1854263.
- aggregation isDescribedBy 1854252.
- aggregation similarTo cr.2011.49.
- aggregation similarTo LU-1854252.