The DOI matches its Crossref record; 85 of the 85 references it cites were found in a registry or an index.
Megalin and cubilin: synergistic endocytic receptors in renal proximal tubule
Abstract
The multiligand, endocytic receptors megalin and cubilin are colocalized in the renal proximal tubule. They are heavily expressed in the apical endocytic apparatus. Megalin is a 600-kDa transmembrane protein belonging to the low-density lipoprotein-receptor family. The cytoplasmic tail contains three NPXY motifs that mediate the clustering in coated pits and are possibly involved in signaling functions. Cubilin, also known as the intestinal intrinsic factor-cobalamin receptor, is a 460-kDa receptor with no transmembrane domain and no known signal for endocytosis. Because the two receptors bind each other with high affinity and colocalize in several tissues, it is highly conceivable that megalin mediates internalization of cubilin and its ligands. Both receptors are important for normal tubular reabsorption of proteins, including albumin. Among the proteins normally filtered in the glomeruli, cubilin has been shown to bind albumin, immunoglobulin light chains, and apolipoprotein A-I. The variety of filtered ligands identified for megalin include vitamin-binding proteins, hormones, enzymes, apolipoprotein H, albumin, and β 2- and α 1-microglobulin. Loss of these proteins and vitamins in the urine of megalin-deficient mice illustrates the physiological importance of this receptor.
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Haraldsson, B., Nyström, J., & Deen, W. M. (2008) · Physiological Reviews · doi:10.1152/physrev.00055.2006 · Cited by 909
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Chun, R. F., Peercy, B. E., Orwoll, E. S., Nielson, C. M., Adams, J. S., & Hewison, M. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2013.09.012 · Cited by 448
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Metadata
- Authors
- Christensen, E. I., & Birn, H.
- Venue
- American Journal of Physiology-Renal Physiology
- Publisher
- American Physiological Society
- Published
- 2001-04-01
- Volume
- 280
- Issue
- 4
- Pages
- F562-F573
- ISSN
- 1522-1466 (ISSN-L)
- 1931-857X
- OpenAlex
- W2161824703
- Cited by
- 379
- References
- 85
- FWCI
- 12.97
- Type
- journal article
- Language
- en
- Open access
- closed
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