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   <subfield code="a">Atypical PKC phosphorylates microtubule affinity-regulating kinase 4 in vitro</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Farha Naz, Asimul Islam, Faizan Ahmad, Md. Hassan]</subfield>
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   <subfield code="a">MAP/Microtubule affinity-regulating kinase 4 (MARK4), a Ser/Thr protein kinases, is related to the Par-1 (partitioning-defective) gene products, and is the human ortholog of Par-1. MARK4 shows its role in the cell polarity at the time of embryonic development. It is mostly located at the basal regionof cells, providing apico-basal polarity. Here, we made two variants of human Par-1d (MARK4), kinase domain (MARK4-F2), and kinase domain along with 59N-terminal residues (MARK4-F1) and saw their ATPase hydrolysis in the presence of each other. We observed that the activity of one variant was increased in the presence of other. We also demonstrated that both variants were phosphorylated by atypical PKC and their activities were increased in the presence of increasing concentration of atypical protein kinase c (aPKC). The phosphorylation was observed at the serine and threonine residues of MARK4. The interaction of MARK2 and MARK3 with aPKC and their negative regulation by aPKC is already known. This study confirms a functional link between aPKC and MARK4, two central determinants of cell polarity, and it suggests that aPKC may regulate all four members of Par-1 through phosphorylating them in polarized cells.</subfield>
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   <subfield code="a">Springer Science+Business Media New York, 2015</subfield>
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   <subfield code="a">Cell polarity</subfield>
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   <subfield code="a">ATP</subfield>
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   <subfield code="u">Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, 110025, New Delhi, India</subfield>
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   <subfield code="t">Molecular and Cellular Biochemistry</subfield>
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   <subfield code="g">410/1-2(2015-12-01), 223-228</subfield>
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   <subfield code="a">Metadata rights reserved</subfield>
   <subfield code="b">Springer special CC-BY-NC licence</subfield>
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