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Am J Physiol Renal Physiol 281: F995-F1018, 2001;
0363-6127/01 $5.00
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Vol. 281, Issue 6, F995-F1018, December 2001

INVITED REVIEW
Heteromeric amino acid transporters: biochemistry, genetics, and physiology

Josep Chillarón1, Ramón Roca2, Alfonso Valencia2, Antonio Zorzano1, and Manuel Palacín1

1 Departament de Bioquimica i Biologia Molecular, Facultat de Biologia, Universitat de Barcelona, Barcelona E-08028; and 2 Protein Design Group, Centro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas, Madrid E-28049, Spain

The heteromeric amino acid transporters (HATs) are composed of two polypeptides: a heavy subunit (HSHAT) and a light subunit (LSHAT) linked by a disulfide bridge. HSHATs are N-glycosylated type II membrane glycoproteins, whereas LSHATs are nonglycosylated polytopic membrane proteins. The HSHATs have been known since 1992, and the LSHATs have been described in the last three years. HATs represent several of the classic mammalian amino acid transport systems (e.g., L isoforms, y+L isoforms, asc, x<UP><SUB>c</SUB><SUP>−</SUP></UP>, and b0,+). Members of the HAT family are the molecular bases of inherited primary aminoacidurias cystinuria and lysinuric protein intolerance. In addition to the role in amino acid transport, one HSHAT [the heavy subunit of the cell-surface antigen 4F2 (also named CD98)] is involved in other cell functions that might be related to integrin activation. This review covers the biochemistry, human genetics, and cell physiology of HATs, including the multifunctional character of CD98.

light and heavy subunits; cystinuria; lysinuric protein intolerance; CD98 (4F2) complex and integrins; rBAT


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