High impact information on AP4M1

• Furthermore, in MDCK cells with depleted mu 4 protein levels, several basolateral proteins are mis-sorted to the apical surface, showing that AP-4 participates in basolateral sorting in epithelial cells [1].
• In contrast, mu4 binds equally well to the GTP- and GDP-bound forms of ARF1 and is less dependent on switch I and switch II residues [2].
• This complex consists of four subunits (epsilon, beta4, mu4 and sigma4) and localizes to the cytoplasmic face of the trans-Golgi network (TGN) [2].
• The mu4 subunit of the complex specifically interacts with a tyrosine-based sorting signal, indicating that, like the other three AP complexes, AP-4 is involved in the recognition and sorting of cargo proteins with tyrosine-based motifs [3].
• Addition of Co(NH3)6(3+) to aqueous solutions of Cu(II) in excess carbonate promotes the assembly of a new highly charged carbonato-copper(II) anion, [Cu4(OH)(CO3)8](9-), which contains an unusual mu4 hydroxo-bridged square Cu4 arrangement, stabilised in the crystal by no less than forty hydrogen bonds (< 3 Angstrom) to hexammine cations [4].

Anatomical context of AP4M1

• The mRNAs of both molecules are expressed in all tissues analyzed, but with different profiles of relative abundance. mu-ARP1 is most abundant in brain, ovary and lung, whereas mu-ARP2 is prominently expressed in testis [5].

Associations of AP4M1 with chemical compounds

• High-nuclearity ruthenium carbonyl cluster complexes derived from 2-amino-6-methylpyridine: synthesis of nonanuclear derivatives containing mu4- and mu5-oxo ligands [6].
• Luminescent silver metal chains with unusual mu4-bonded 2,2'-bipyrazine [7].

Other interactions of AP4M1

• In addition, we demonstrate a direct interaction of the epsilon and mu4 subunits of AP-4 with ARF1. epsilon binds only to ARF1-GTP and requires residues in the switch I and switch II regions of ARF1 [2].

References