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anti-Human SLC36A1 Antibodies:
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A mechanism through which amino acids may suppress the expression of PAT1 on lysosomes by inducing protein cleavage to remove a targeting signal.
Data indicate that the glycosylation-deficient mutant of amino acid transporter PAT1 (PAT1(3)(NQ) ) is unstable and is degraded mainly via the endoplasmic reticulum-associated degradation pathway in HEK293 cells.
Sertraline is an apparent non-competitive inhibitor of PAT1-mediated transport.
Data suggest that PAT1 in enterocytes is responsible for intestinal absorption of some of the alkaloids from areca nut (i.e., arecaidine, guvacine, isoguvacine).
estrogen attenuates the activity of PAT1 by directly closing PAT1
In hPAT1 expressing oocytes Gly-Tyr, Gly-Pro, and Gly-Phe inhibited currents induced by drug substances.
PATs function as part of an amino acid-sensing engine that drives mTORC1 activation from endosomal and lysosomal membranes
In human cells, SLC36A1 localized on intracellular membranes is required for amino acid-dependent mTORC1 activation and cell proliferation. SLC36A1 also has similar in vivo growth regulatory activity to fly SLC36 AAAPs when expressed in Drosophila.
PAT1 expressed exclusively in apical membrane of Caco-2 cells. hPAT1 may be responsible for H(+)-coupled amino acid transport expressed in apical membrane of Caco-2 cells.
A high-capacity imino acid carrier localized at the small intestinal luminal membrane that transports nutrients and amino acids and imino acids.
Amino acid uptake via hPAT1 is inhibited by activators of the cAMP pathway indirectly through inhibition of NHE3 activity.
PAT1a, which is 99.0% identical to protein interacting with APP tail 1 (PAT1), is a functional link between the transport and processing of beta-amyloid precursor protein APP and its two paralogs APLP1 and APLP2 in vivo.
His-55 might be responsible for binding and translocation of H+ in the course of cellular amino acid uptake by PAT1.
This study is the first to demonstrate both taurine uptake via PAT1 and functional expression of PAT1 at the apical membrane of the intestinal epithelium.
Data conclude that hPAT1 might be responsible for the intestinal absorption of beta-GPA thereby allowing its oral administration.
The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1
a disulfide bridge is essential for the transport function of the human proton-coupled amino acid transporter hPAT1
Data suggest that a high-fat diet induces expression of two amino acid transporters (Slc36a1, Slc6a20a) in intestinal mucosa pointing to a specific and adaptive absorption of some amino acids in high-fat diet-induced obesity and glucose intolerance.
detailed analysis of the transport mode of the murine PAT1 in oocytes; PAT1 is an electrogenic H+-coupled amino acid symporter with the capability for bidirectional amino acid transport
The essential role of chloride and fructose absorbing Slc36a1 is reported.
This gene encodes a member of the eukaryote-specific amino acid/auxin permease (AAAP) 1 transporter family. The encoded protein functions as a proton-dependent, small amino acid transporter. This gene is clustered with related family members on chromosome 5q33.1.
, lysosomal amino acid transporter 1
, proton-coupled amino acid transporter 1
, proton/amino acid transporter 1
, solute carrier family 36 member 1
, neutral amino acid/proton symporter
, ysosomal amino acid transporter 1