Disease relevance of TAT1

• The second system studied consisted of the (+18)-(+44) fragment of the trans-activation response element of human immunodeficiency virus type 1 (TAR RNA HIV-1) and a 9-amino-acid peptide of the trans-activator of transcription protein (Tat HIV-1) Tat(49-57)-NH(2) (named Tat1: Arg(49)-Lys-Lys-Arg(52)-Arg-Gln-Arg-Arg- Arg(57)-NH(2)) [1].

High impact information on TAT1

• The HPG1 mutation or the bul1Delta bul2Delta double mutation caused a marked increase in the steady-state level of Tat2 but not of Tat1, although both permeases were degraded at high pressure in an Rsp5-dependent manner [2].
• Moreover, Tat1 was associated with lipid rafts, whereas Tat2 localized in bulk lipids [2].
• Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1 and TAT2, encode amino acid permeases mediating tyrosine and tryptophan uptake [3].
• Antitubulin TAT1 antibody revealed a microtubular cytoskeleton consisting of cytoplasmic and spindle microtubules [4].
• Sequencing of the inserts revealed the presence of the HIP1 gene and also the presence of the TAT1 gene [5].

Biological context of TAT1

• The transporter associated with antigen processing (TAP1 and TAP2) constitute a key machinery in the major histocompatibility complex (MHC) class I-mediated cellular immune defense against infected or malignantly transformed cells [6].

Anatomical context of TAT1

• Tat1 localized predominantly in the plasma membrane, whereas Tat2 was abundant in the internal membranes [2].

Associations of TAT1 with chemical compounds

• Our results suggest that the TAT1-encoded protein, previously characterized as the high-affinity tyrosine permease, also acts as the low affinity histidine permease [5].
• TAT1 encodes a low-affinity histidine transporter in Saccharomyces cerevisiae [5].
• TAT1 is the tyrosine high-affinity transporter, which also mediates low-affinity or low-capacity uptake of tryptophan [3].
• In addition, a close inspection of TAT1 and TAT2 transporters following exposure to phytosphingosine indicates that TAT1 protein is degraded in a similar fashion upon treatment with FTY720 and phytosphingosine [7].

References