Abstract:
:The rat synapse associated protein SAP90 is a member of a superfamily of potential guanylate kinases localized at cell-cell contact sites. This superfamily includes the synapse associated protein SAP97, a close relative of SAP90, the Drosophila tumor suppressor gene product dlg-Ap, the mammalian zonula occludens proteins ZO-1 and ZO-2 and the erythrocyte protein p55. Here we show that SAP90 specifically binds GMP in the micromolar range while binding to ATP, GDP and ADP is at a much lower affinity (10-25 mM), whether or not binding is detected for other guanine and adenine nucleotides. No guanylate kinase activity of SAP90 was detected under our experimental conditions. The importance of the GMP binding capacity per se and an evolutionary role for conserving of the guanylate kinase domain in this superfamily are discussed.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kistner U,Garner CC,Linial Mdoi
10.1016/0014-5793(95)00030-dsubject
Has Abstractpub_date
1995-02-13 00:00:00pages
159-63issue
2-3eissn
0014-5793issn
1873-3468journal_volume
359pub_type
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