{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T05:13:24Z","timestamp":1791090804761,"version":"4.1.0"},"reference-count":50,"publisher":"The Company of Biologists","issue":"15","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2002,8,1]]},"abstract":"<jats:p>S100 proteins have attracted great interest in recent years because of their cell- and tissue-specific expression and association with various human pathologies. Most S100 proteins are small acidic proteins with calcium-binding domains \u2014 the EF hands. It is thought that this group of proteins carry out their cellular functions by interacting with specific target proteins, an interaction that is mainly dependent on exposure of hydrophobic patches, which result from calcium binding. S100A13, one of the most recently identified members of the S100 family, is expressed in various tissues. Interestingly,hydrophobic exposure was not observed upon calcium binding to S100A13 even though the dimeric form displays two high- and two low- affinity sites for calcium. Here, we followed the translocation of S100A13 in response to an increase in intracellular calcium levels, as protein translocation has been implicated in assembly of signaling complexes and signaling cascades, and several other S100 proteins are involved in such events. Translocation of S100A13 was observed in endothelial cells in response to angiotensin II, and the process was dependent on the classic Golgi-ER pathway. By contrast, S100A6 translocation was found to be distinct and dependent on actin-stress fibers. These experiments suggest that different S100 proteins utilize distinct translocation pathways, which might lead them to certain subcellular compartments in order to perform their physiological tasks in the same cellular environment.<\/jats:p>","DOI":"10.1242\/jcs.115.15.3149","type":"journal-article","created":{"date-parts":[[2021,4,25]],"date-time":"2021-04-25T17:33:08Z","timestamp":1619371988000},"page":"3149-3158","source":"Crossref","is-referenced-by-count":41,"title":["S100A13 and S100A6 exhibit distinct translocation pathways in endothelial cells"],"prefix":"10.1242","volume":"115","author":[{"given":"Hsiao-Ling","family":"Hsieh","sequence":"first","affiliation":[{"name":"Department of Pediatrics, Division of Clinical Chemistry and Biochemistry,University of Zurich, Steinwiesstr. 75, CH-8032 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beat W.","family":"Scha\u0308fer","sequence":"additional","affiliation":[{"name":"Department of Pediatrics, Division of Clinical Chemistry and Biochemistry,University of Zurich, Steinwiesstr. 75, CH-8032 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos A.","family":"Cox","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, 30, quai Ernest Ansermet, CH-1211 Gene\u0300ve 4,Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claus W.","family":"Heizmann","sequence":"additional","affiliation":[{"name":"Department of Pediatrics, Division of Clinical Chemistry and Biochemistry,University of Zurich, Steinwiesstr. 75, CH-8032 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2021042517215133200_REF1","doi-asserted-by":"crossref","unstructured":"Brett, W., Mandinova, A., Remppis, A., Sauder, U., Ruter, F.,Heizmann, C. 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R., Crescenzi, O., Weber, C., Lubienski,M. J., Hidaka, H. and Chazin, W. J. (1998). The three-dimensional structure of Ca(2+)-bound calcyclin: implications for Ca(2+)-signal transduction by S100 proteins. Structure6, 223-231.","DOI":"10.1016\/S0969-2126(98)00023-9"},{"key":"2021042517215133200_REF38","doi-asserted-by":"crossref","unstructured":"Scha\u0308fer, B. W. and Heizmann, C. W. (1996). The S100 family of EF-hand calcium-binding proteins: functions and pathology.Trends Biochem. Sci.21, 134-140.","DOI":"10.1016\/0968-0004(96)10020-7"},{"key":"2021042517215133200_REF39","doi-asserted-by":"crossref","unstructured":"Scha\u0308fer, B. W., Wicki, R., Engelkamp, D., Mattei, M. G. and Heizmann, C. W. (1995). Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium- binding protein family.Genomics25, 638-643.","DOI":"10.1016\/0888-7543(95)80005-7"},{"key":"2021042517215133200_REF40","doi-asserted-by":"crossref","unstructured":"Scha\u0308fer, B. W., Fritschy, J. M., Murmann, P., Troxler, H.,Durussel, I., Heizmann, C. W. and Cox, J. A. (2000). Brain S100A5 is a novel calcium-, zinc-, and copper ion-binding protein of the EF-hand superfamily. J. Biol. Chem.275, 30623-30630.","DOI":"10.1074\/jbc.M002260200"},{"key":"2021042517215133200_REF41","unstructured":"Schiffrin, E. L. (1998). Vascular protection with newer antihypertensive agents. J. Hypertens. Suppl.16, S25-S29."},{"key":"2021042517215133200_REF42","doi-asserted-by":"crossref","unstructured":"Shishibori, T., Oyama, Y., Matsushita, O., Yamashita, K.,Furuichi, H., Okabe, A., Maeta, H., Hata, Y. and Kobayashi, R.(1999). Three distinct anti-allergic drugs, amlexanox, cromolyn and tranilast, bind to S100A12 and S100A13 of the S100 protein family.Biochem. J.338, 583-589.","DOI":"10.1042\/bj3380583"},{"key":"2021042517215133200_REF43","doi-asserted-by":"crossref","unstructured":"Stradal, T. B. and Gimona, M. (1999). Ca2+-dependent association of S100A6 (Calcyclin) with the plasma membrane and the nuclear envelope. J. Biol. Chem.274, 31593-31596.","DOI":"10.1074\/jbc.274.44.31593"},{"key":"2021042517215133200_REF44","unstructured":"Takeuchi, K. (1999). [Signal transduction systems of angiotensin II receptors]. Nippon Rinsho.57, 1070-1077."},{"key":"2021042517215133200_REF45","doi-asserted-by":"crossref","unstructured":"Tarantini, F., Micucci, I., Bellum, S., Landriscina, M.,Garfinkel, S., Prudovsky, I. and Maciag, T. (2001). The precursor but not the mature form of IL1alpha blocks the release of FGF1 in response to heat shock. J. Biol. 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