Functional analysis of the guanylate kinase-like domain in the synapse-associated protein SAP97

European Journal of Biochemistry
S KuhlendahlC C Garner

Abstract

SAP97 is a membrane cytoskeletal protein localized at the presynaptic nerve terminals of type 1 asymmetric synapses. It has been implicated in the assembly of synapses and in particular in the localization and clustering of ion channels. The C-terminal GK domain of SAP97 shares a high degree of sequence similarity with low-molecular-mass guanylate kinases. These enzymes are involved in the guanine nucleotide metabolic cycle and in the maintenance of GTP/GDP pools required for example in Ras-mediated cell signaling. It has therefore been hypothesized that SAP97 plays an essential role in cellular signaling by regulating the guanine nucleotide pools at synaptic junctions. Here, we test this hypothesis by assessing whether the GK domain in SAP97 encodes an authentic guanylate kinase. We show that the GK domain in and of itself does not encode an active guanylate kinase, that it cannot be activated by its binding partner GKAP and that flanking regions are not acting as inhibitory regulators for enzymatic activity. Thus, it would appear that the GK domain of SAP97 is not involved in the metabolism of guanine nucleotides required for signaling events.

Citations

Jun 17, 2000·Trends in Cell Biology·C C GarnerR L Huganir
Sep 23, 2009·Biochemistry·Jana MarcetteKenneth E Prehoda
Nov 4, 2000·The EMBO Journal·H WuC C Garner
Jun 15, 2005·Annual Review of Biochemistry·Lars FunkeDavid S Bredt
Jun 9, 2000·Annual Review of Physiology·M Sheng, D T Pak
Jul 9, 2011·Developmental Neurobiology·Carlos OlivaJimena Sierralta
Dec 1, 2001·The Journal of Biological Chemistry·Yuanhe LiArnon Lavie
Dec 18, 2001·The Journal of Biological Chemistry·Andrea PiserchioDale F Mierke
Mar 11, 2000·American Journal of Physiology. Renal Physiology·S W StraightJ B Wade
Oct 22, 2008·Biochimica Et Biophysica Acta·Anne-Laure SurenaMarie-Pierre Junier

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