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245 1 0 _aFAB1C, a phosphatidylinositol 3-phosphate 5-kinase, interacts with PIN-FORMEDs and modulates their lytic trafficking in Arabidopsis
490 0 _vProceedings of the National Academy of Sciences, 120(46), p.e2310126120, 2023
520 3 _aPIN-FORMEDs (PINs)are auxin efflux carriers that asymmetrically target the plasma membrane (PM)and are critical for forming local auxin gradients and auxin responses. While the cytoplasmic hydrophilic loop domain of PIN (PIN-HL)is known to include some molecular cues (e.g., phosphorylation)for the modulation of PIN's intracellular trafficking and activity, the complexity of auxin responses suggests that additional regulatory modules may operate in the PIN-HL domain. Here, we have identified and characterized a PIN-HL-interacting protein (PIP)called FORMATION OF APLOID AND BINUCLEATE CELL 1C (FAB1C), a phosphatidylinositol-3-phosphate 5-kinase, which modulates PIN's lytic trafficking. FAB1C directly interacts with PIN-HL and is required for the polarity establishment and vacuolar trafficking of PINs. Unphosphorylated forms of PIN2 interact more readily with FAB1C and are more susceptible to vacuolar lytic trafficking compared to phosphorylated forms. FAB1C also affected lateral root formation by modulating the abundance of periclinally localized PIN1 and auxin maximum in the growing lateral root primordium. These findings suggest that a membrane-lipid modifier can target the cargo-including vesicle by directly interacting with the cargo and modulate its trafficking depending on the cargo's phosphorylation status.
650 1 4 _aFAB1
650 1 4 _aPIN-FORMED (PIN)
650 1 4 _aAUXIN TRANSPORT
650 1 4 _aENDOMEMBRANE TRAFFICKING
650 1 4 _aPHOSPHATIDYLINOSITOL-3-PHOSPHATE 5-KINASE
700 1 2 _aMaeng, K. H.
700 1 2 _aLee, H.
700 1 2 _aCho, H. T.
856 4 0 _uhttps://drive.google.com/file/d/13FHRBWO1Kf7SDStkXy6pH6-bDfr_gKv5/view?usp=drivesdk
_zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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