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. Author manuscript; available in PMC: 2012 Aug 24.
Published in final edited form as: Biochim Biophys Acta. 2008 Jul 23;1781(10):610–617. doi: 10.1016/j.bbalip.2008.07.002

Fig. 5.

Fig. 5

Analysis of potentially important domains for the differential localization of SMS1 and SMS2. (A) Schematic of the Flag-tagged constructs used. SAM: Sterile Alpha Motif. TM: transmembrane domain. (B) SMS1ΔSAM-Flag, a mutant with truncation of the first 61 amino acids from SMS1, shows no defect in SMS activity compared with WT SMS1-Flag. Likewise, SAM-SMS2, a fusion protein comprised of the SAM domain from SMS1 (amino acids 1-61) and the entirety of SMS2, has unaltered SMS activity compared to WT-SMS2-Flag. The protein levels of each enzyme is shown at the bottom. (C) SMS1ΔSAM-Flag remains as a Golgi targeted protein. α Mannosidase II is depicted in green, while SMS1ΔSAM-Flag is depicted in red. TOPRO-3 is in blue. (D) SAM-SMS2-Flag exhibits an identical localization pattern compared to wild type SMS2. Cadherin is depicted in green, while SAM-SMS2-Flag is depicted in red. TOPRO-3 is in blue.