High impact information on ANXA13

• Using immobilized Nedd4-C2 domain to trap interacting proteins from MDCK cell lysate, we isolated, in the presence of Ca(2+), a approximately 35-40-kD protein that we identified as annexin XIII using mass spectrometry [1].
• In vitro studies using an octapeptide derived from residues 2-9 of the primary translation product of ISA mRNA and purified myristoyl-CoA:protein N-myristoyltransferase suggested that it is N-myristoylated [2].
• In polarized enterocytes, the highest concentrations of ISA are found at the apical compared to basolateral membrane [2].
• The restricted cellular expression and acylation of ISA distinguish it from other known annexins.(ABSTRACT TRUNCATED AT 400 WORDS)[2]
• In vivo labeling studies confirmed that myristate is covalently attached to ISA via a hydroxylamine resistant amide linkage [2].

Biological context of ANXA13

• Genomic locations of ANX11 and ANX13 and the evolutionary genetics of human annexins [3].
• This contrasts with an earlier observation for ISU-mediated cluster assembly [Wu, S., et al. (2002) Biochemistry 41, 8876-8885], where the rates differed for Hs and Sp target Fd's, suggesting distinct binding sites for binding of holo ISA and ISU to apo Fd [4].

Anatomical context of ANXA13

• Immunocytochemical studies reveal that the intestine-specific annexin (ISA) is associated with the plasma membrane of undifferentiated, proliferating crypt epithelial cells as well as differentiated villus enterocytes [2].

Associations of ANXA13 with chemical compounds

• Minor variations in rate constant for the ISA Cys derivatives do not reflect any change in the affinity of binding to the apo Fd since k(2) was found to be independent of the concentration of apo Fd over the range of 1-25 microM [4].
• The relative effectiveness of the ISA enantiomers was determined and compared to the achiral synthetic auxin indole-3-butyric acid and to the natural auxin indole-3-acetic acid [5].

Other interactions of ANXA13

• Conversely, a tandem pair of novel annexins from the amphioxus Branchiostoma floridae resembled annexin A13 in gene structure and conserved the charged amino acids associated with the internal hydrophilic pore, but were devoid of external type 2 calcium-binding sites and incorporated K/RGD motifs instead, like annexin A9 [6].

References