MAGI-1, a Membrane-associated Guanylate Kinase with a Unique Arrangement of Protein-Protein Interaction Domains

Membrane-associated guanylate kinase (MAGUK) proteins participate in the assembly of multiprotein complexes on the inner surface of the plasma membrane at regions of cell-cell contact. MAGUKs are characterized by three types of protein-protein interaction modules: the PDZ domain, the Src homology 3 (SH3) domain, and the guanylate kinase (GuK) domain. The arrangement of these domains is conserved in all previously known MAGUKs: either one or three PDZ domains in the NH2-terminal half, followed by the SH3 domain, followed by a COOH-terminal GuK domain. In this report, we describe the cDNA cloning and subcellular distribution of MAGI-1, a MAGUK with three unique structural features: 1) the GuK domain is at the NH2 terminus, 2) the SH3 domain is replaced by two WW domains, and 3) it contains five PDZ domains. MAGI-1 mRNA was detected in several adult mouse tissues. Sequence analysis of overlapping cDNAs revealed the existence of three splice variants that are predicted to encode MAGI-1 proteins with different COOH termini. The longest variant, MAGI-1c, contains three bipartite nuclear localization signals in its unique COOH-terminal sequence and was found predominantly in the nucleus of Madin-Darby canine kidney cells. A shorter form lacking these signals was found primarily in membrane and cytoplasmic fractions. This distribution, which is reminiscent of that seen for the tight junction protein ZO-1, suggests that MAGI-1 may participate in the transmission of regulatory signals from the cell surface to the nucleus. Membrane-associated guanylate kinase (MAGUK) proteins participate in the assembly of multiprotein complexes on the inner surface of the plasma membrane at regions of cell-cell contact. MAGUKs are characterized by three types of protein-protein interaction modules: the PDZ domain, the Src homology 3 (SH3) domain, and the guanylate kinase (GuK) domain. The arrangement of these domains is conserved in all previously known MAGUKs: either one or three PDZ domains in the NH2-terminal half, followed by the SH3 domain, followed by a COOH-terminal GuK domain. In this report, we describe the cDNA cloning and subcellular distribution of MAGI-1, a MAGUK with three unique structural features: 1) the GuK domain is at the NH2 terminus, 2) the SH3 domain is replaced by two WW domains, and 3) it contains five PDZ domains. MAGI-1 mRNA was detected in several adult mouse tissues. Sequence analysis of overlapping cDNAs revealed the existence of three splice variants that are predicted to encode MAGI-1 proteins with different COOH termini. The longest variant, MAGI-1c, contains three bipartite nuclear localization signals in its unique COOH-terminal sequence and was found predominantly in the nucleus of Madin-Darby canine kidney cells. A shorter form lacking these signals was found primarily in membrane and cytoplasmic fractions. This distribution, which is reminiscent of that seen for the tight junction protein ZO-1, suggests that MAGI-1 may participate in the transmission of regulatory signals from the cell surface to the nucleus. The prototypical members of the membrane-associated guanylate kinase (MAGUK) 1The abbreviations used are: MAGUK, membrane-associated guanylate kinase; DLG, discs large; hDLG, human DLG; SH3, Src homology 3; GuK, guanylate kinase; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; GST, glutathioneS-transferase; MDCK, Madin-Darby canine kidney; bp, base pair(s); kb, kilobase pair(s); hYAP, human YAP65. family are the Drosophila tumor suppressor protein DLG, the erythrocyte membrane protein p55, and the neuronal protein PSD-95/SAP90 (1Anderson J.M. Balda M.S. Fanning A.S. Curr. Opin. Cell Biol. 1993; 5: 772-778Crossref PubMed Scopus (181) Google Scholar, 2Kim S.K. Curr. Opin. Cell Biol. 1995; 7: 641-649Crossref PubMed Scopus (99) Google Scholar). These proteins share a common modular structure that consists of either one or three PDZ domains, a single Src homology 3 (SH3) domain, and a single region of homology to Saccharomyces cerevisiaeguanylate kinase (GuK), known as the GuK domain. The MAGUK family includes the epithelial tight junction proteins ZO-1 and ZO-2, theCaenorhabditis elegans vulval protein LIN-2A, and the neurexin-binding protein CASK (3Anderson J.M. Curr. Biol. 1996; 6: 382-384Abstract Full Text Full Text PDF PubMed Scopus (219) Google Scholar, 4Hoskins R. Hajnal A.F. Harp S.A. Kim S.K. Development. 1996; 122: 97-111Crossref PubMed Google Scholar, 5Hata Y. Butz S. Sudhof T.C. J. Neurosci. 1996; 16: 2488-2494Crossref PubMed Google Scholar). The latter two represent a subfamily of MAGUKs characterized by an additional domain at the NH2 terminus that is similar to calmodulin kinase II. All MAGUKs studied to date localize to regions of cell-cell contact, such as tight junctions in epithelial cells and synaptic junctions in neurons, where they nucleate the assembly of multiprotein complexes via their protein-protein interaction domains (6Gomperts S.N. Cell. 1996; 84: 659-662Abstract Full Text Full Text PDF PubMed Scopus (223) Google Scholar, 7Fanning A.S. Anderson J.M. Curr. Biol. 1996; 6: 1385-1388Abstract Full Text Full Text PDF PubMed Scopus (243) Google Scholar). In addition, ZO-1 was found in the nucleus of cultured cells under certain growth conditions (8Gottardi C.J. Arpin M. Fanning A.S. Louvard D. Proc. Natl. Acad. Sci. U. S. A. 1996; 93: 10779-10784Crossref PubMed Scopus (305) Google Scholar). PSD-95/SAP90 is the prototype of a subfamily of neuronal MAGUKs that includes SAP97/hDLG, chapsyn-110/PSD-93, and SAP102 (9Cho K.O. Hunt C.A. Kennedy M.B. Neuron. 1992; 9: 929-942Abstract Full Text PDF PubMed Scopus (1008) Google Scholar, 10Brenman J.E. Christopherson K.S. Craven S.E. McGee A.W. Bredt D.S. J. Neurosci. 1996; 16: 7407-7415Crossref PubMed Google Scholar, 11Kim E. Cho K.O. Rothschild A. Sheng M. Neuron. 1996; 17: 103-113Abstract Full Text Full Text PDF PubMed Scopus (476) Google Scholar, 12Kistner U. Wenzel B.M. Veh R.W. Cases-Langhoff C. Garner A.M. Appeltauer U. Voss B. Gundelfinger E.D. Garner C.C. J. Biol. 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The latter the that PDZ domain proteins the of multiprotein complexes via interaction of their PDZ domains with (3Anderson J.M. Curr. Biol. 1996; 6: 382-384Abstract Full Text Full Text PDF PubMed Scopus (219) Google Scholar). The of the PDZ domain of and of the PDZ domain of to a C. S. 1996; PubMed Scopus Google Scholar, A. J. Kim E. Sheng M. R. Cell. 1996; Full Text Full Text PDF PubMed Scopus Google Scholar). This with in Fanning A.S. C. J. A. Anderson J.M. PubMed Scopus Google to the by which is in PDZ domain of PDZ domains, in the COOH-terminal that to the is such as found in the The of the or at the in this a with a in that is conserved in PDZ domains A. J. Kim E. Sheng M. R. Cell. 1996; Full Text Full Text PDF PubMed Scopus Google Scholar). The single PDZ domains in and a in of the and these domains in that in the Fanning A.S. C. J. A. Anderson J.M. PubMed Scopus Google Scholar). The PDZ domain of neuronal a in which the is replaced by a complexes with PDZ domains, the neuronal PDZ domain to in that in the sequence Christopherson K.S. R.W. Bredt D.S. M. 15: PubMed Scopus Google Scholar). a single in PDZ domain to in may which is found in the of its structural of PDZ domains are predicted to in a to the of a COOH-terminal sequence as a C. S. 1996; PubMed Scopus Google Scholar, A. J. Kim E. Sheng M. R. Cell. 1996; Full Text Full Text PDF PubMed Scopus Google Scholar, Fanning A.S. C. J. A. Anderson J.M. PubMed Scopus Google Scholar). with that are to the additional GuK domains in MAGUKs of their GuK, which to and A. E. J. PubMed Scopus Google Scholar). of GuK domains found in MAGUKs: that the and and in which the are conserved the is and that the and LIN-2A, and U. Garner C.C. M. 1995; PubMed Scopus Google Scholar). of the GuK domains in MAGUK proteins are known to A to the of the GuK domain in MAGUK proteins two a synaptic by one and by the which to the GuK domains of the proteins E. S. A. Rothschild A. A.M. Sheng M. J. Cell Biol. PubMed Scopus Google Scholar, M. Y. A. M. Y. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). was found in a with and that it may to this in the it is known the interaction and is by this suggests that the GuK domains in MAGUK proteins may as for protein-protein A protein-protein interaction that previously found in MAGUK proteins is the WW domain D. Curr. Biol. 1996; Scholar, M. Sci. 1996; Full Text PDF PubMed Scopus Google Scholar). The WW domain was for two conserved and was first as two in mouse of M. A. M. D. J. Biol. Chem. 1995; Full Text Full Text PDF PubMed Scopus Google Scholar). WW domains by sequence in proteins from and by WW domains in human such as and M. Biol. 1996; PubMed Scopus Google Scholar). and are for the single WW domain in human M. Proc. Natl. Acad. Sci. U. S. A. 1995; PubMed Scopus Google Scholar). These proteins to the WW domain via that to the sequence the the WW domains in proteins to a sequence in that the that all WW domains to this J. 1996; 15: PubMed Scopus Google Scholar). The the WW domain and a SH3 domain the that these two domains may with one for the of the in a its interaction with the WW domain, a regulatory for WW domain A. E. S. M. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). In this report, we describe a MAGUK with three that it from all known members of the 1) the GuK domain is at the NH2 terminus at the COOH 2) the SH3 domain is replaced by two WW and 3) it contains five PDZ domains the one or This protein MAGI-1, guanylate kinase with an arrangement of protein-protein interaction domains. The the and and the mouse cDNA in Cell. 1993; Full Text PDF PubMed Scopus Google from of the of at by of the and The of was the in and was by a of was for in and with the and for an additional 3 by in and by two followed by in the of The was for at the was to a and the protein of was with the protein of protein from was to a of with and with of from the a at at which was in a the by in a by the in of protein from a of The cDNA was from by with and with the This was used to an mouse cDNA in to the MAGI-1 cDNAs from a of MAGI-1 cDNAs in a similar from an mouse The of cDNA was by and by and The cDNA was on A of MAGI-1, was with and used to a mouse The was used at a of in to the to for the the was and with a glyceraldehyde-3-phosphate A that of MAGI-1 was by and the and The and protein was and by and used to as previously Anderson M.S. J. Biol. Chem. Full Text PDF PubMed Google Scholar, M.S. J. Biol. Chem. 1995; Full Text Full Text PDF PubMed Scopus Google Scholar). was and by and the was with as previously Anderson M.S. J. Biol. Chem. Full Text PDF PubMed Google was by of to and was as previously Anderson M.S. J. Biol. Chem. Full Text PDF PubMed Google Scholar). was from from the by on protein A was by with a to of mouse that to and was from by on protein All used at a of the previously M.S. J. Biol. Chem. 1993; 268: Full Text PDF PubMed Google was used at a of A of the the was the and the was of this with a from the of the which was replaced by the region from the of human kidney cells with of as previously Anderson M.S. J. Biol. Chem. Full Text PDF PubMed Google Scholar). a in A and the protein of was as of protein from was to and to analysis with the as previously M.S. J. Biol. Chem. Full Text PDF PubMed Google Scholar). cells in and on at a of and on 3 by in Cell in and by in a on The was at for at and the was to a and the The was in to an additional in a and as The from this was with the and at for at to and fractions. The was in a of and for at The from this was and the was in and the nuclear The protein of was and an of was to followed by analysis with the of to the plasma membrane a COOH-terminal a domain, a of that are from the by C.J. Cell. Full Text PDF PubMed Scopus Google Scholar). The by which these structural to the plasma membrane is used the to for proteins that with the COOH terminus of revealed that to with in the a that was its with is to the where it to in the the used in cDNA a from the COOH terminus of that was A was from a mouse with and with an to with a to with of and a protein that a domain, that its interaction with was A of the sequence of with in revealed a region of that a PDZ domain, which was the to with from the in that was as a for this PDZ domain of with in the of are in the and the from their interaction with and and 2) are in the on the The in and are in as under are as a of the from the interaction of with which was a of and in are in in two in a The of are in the and the from their interaction with and and 2) are in the on the The in and are in as under are as a of the from the interaction of with which was a of and in are in in two the structural of for its interaction with and the from their interaction with was in a a of the COOH-terminal in a in The by similar the COOH-terminal was replaced by or PDZ domain a or three from the COOH terminus to as the which a with a in their PDZ domain A. J. Kim E. Sheng M. R. Cell. 1996; Full Text Full Text PDF PubMed Scopus Google to in the PDZ domain of in was replaced with of a in with 2) its interaction with known PDZ domains in which the COOH-terminal is a Fanning A.S. C. J. A. Anderson J.M. PubMed Scopus Google Scholar). The by in was replaced by of three and in a in that one or in the domain participate in the interaction with of three in a similar in was replaced by and that the the domain and the COOH terminus was in the of a COOH-terminal that to the by PDZ domains. of and in the domain with a in of and and and with in and in A single of with was as as of and All of the with that that to with of in the of the sequence with the sequence of revealed the of in a of that to the the and in These are predicted to in to in the and of a A. J. Kim E. Sheng M. R. Cell. 1996; Full Text Full Text PDF PubMed Scopus Google Scholar). of these with 1) the interaction of with to with the in which was replaced by The cDNA was used as a to several cDNAs from mouse and The longest cDNA to date is in of a region and a followed by a and a region of The a for to and is by in all three This cDNA was from a and and to the of a it a overlapping cDNA was which the region by and in a The of the two overlapping cDNAs is bp, which is with a of that was detected on a This sequence is predicted to encode a protein of with a of distribution of mouse MAGI-1 A mRNA from mouse was with a MAGI-1 as under The was and with a The of is on the for MAGI-1 and for A of the predicted sequence with in the base revealed the of a GuK domain the NH2 terminus, followed by two WW domains and five PDZ domains The MAGI-1 cDNA from the to of the first PDZ domain. in the domain structure of MAGI-1 is unique with members of the MAGUK of a that the GuK domain and the WW domain, are to the predicted sequence of a cDNA that was from a human cDNA via its interaction with that J.M. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). additional of MAGI-1 cDNAs from of an mRNA splice at in the PDZ domain. These cDNAs are predicted to encode proteins of and and and MAGI-1c, The longest cDNA to date contains and was found in a The sequence of this cDNA the GuK domain and with a its is to to it in which may to a of detected in mRNA on a The longest cDNA is in its sequence the and PDZ domains and in the it a it is to the of the from which it it may to either the or the detected on a The COOH-terminal of of and This region contains three bipartite nuclear localization signals J. C. Cell. Full Text PDF PubMed Scopus Google the and of which are overlapping in The distribution of MAGI-1 mRNA was by analysis of mRNA from mouse tissues. A from the of the cDNA to of and in mRNA from and The and detected in and and of the to revealed the and in 3) and of and in that of MAGI-1 in adult is that the of and MAGI-1c, and these human kidney cells. of these cells by with a of This detected proteins of and in cells with and MAGI-1c, and These proteins detected in of cells that with they detected with of and detected in a of cells with 3) with with to seen in cells detected in of mouse and and that they represent of and MAGI-1c, mRNA splice variants unique to cells. on its is to similar to that of their predicted by the protein to as and the protein as was the in mouse primarily and the two in in mouse the subcellular distribution of MAGI-1 proteins in and nuclear and an of was to analysis with was found primarily in the and with a in the nuclear In was found in the nuclear a was detected in the it was from the These on with the nuclear protein and the of a cytoplasmic was detected in the nuclear and was detected in the of cells and In was detected in the sequence revealed that the GuK domain of MAGI-1 is similar to S. GuK a region The to the was to the region to of S. of the MAGI-1 GuK domain an of for in GuK A. E. J. PubMed Scopus Google are and two of the represent the MAGI-1 GuK domain is similar to the GuK domains in and DLG, which the an U. Garner C.C. M. 1995; PubMed Scopus Google Scholar). to the five PDZ domains in MAGI-1, with the of the PDZ domains in and are and to The the PDZ domains MAGI-1 is that domain may with contains in the region that is predicted to form the the and with the that to with the PDZ domains in and The MAGI-1 PDZ domain is to of the that a in the structure of A. J. Kim E. Sheng M. R. Cell. 1996; Full Text Full Text PDF PubMed Scopus Google are conserved in and three of the five are and in are on of a that the COOH-terminal in All five MAGI-1 PDZ domains a in the to and contains a at the to in This is by in and in and in these in the MAGI-1 PDZ domains in unique of for domain. of the five MAGI-1 PDZ domains a at the to in and the contains a at this that of these domains to that or at the A. J. Kim E. Sheng M. R. Cell. 1996; Full Text Full Text PDF PubMed Scopus Google Scholar, Fanning A.S. C. J. A. Anderson J.M. PubMed Scopus Google Scholar). The to the WW domains in MAGI-1, and with the WW domain in human WW domains in mouse and and the first WW domain in and are and to The structure of revealed a that a M. E. J. M. M. 1996; PubMed Scopus Google Scholar). and with on the of the the domain. These three are conserved in MAGI-1 WW domains The of and in form a surface on the of the domain that with the of the The in the MAGI-1 WW domains are either conserved or with similar and these domains to a and the to of are predicted to to the of a WW interaction M. E. J. M. M. 1996; PubMed Scopus Google and several of these in and from the in the of MAGI-1 WW domain to The first PDZ domain of MAGI-1 was on the of its interaction with the COOH terminus of in the This interaction and of These structural are similar to for localization of to the plasma membrane C.J. Cell. Full Text PDF PubMed Scopus Google with a for MAGI-1 in this in cells is by and on its COOH-terminal that the of to in the it is that these the of the interaction and we to an interaction and in of in which contains its of of is for plasma membrane localization or of by that with MAGI-1 in cultured the interaction is for either of these the of the interaction and in the at this we that the interaction in cells. The interaction and in the in the PDZ domain and of and in which is from the COOH-terminal These sequence of was replaced by The in in a region that is predicted to in to in the and in a C. S. 1996; PubMed Scopus Google Scholar, A. J. Kim E. Sheng M. R. Cell. 1996; Full Text Full Text PDF PubMed Scopus Google Scholar). with this we a for sequence in a and contains in the and This to to the PDZ domains in all of which the found in is the known PDZ domain that contains in this several PDZ domains two in this C. S. 1996; PubMed Scopus Google Scholar, A. J. Kim E. Sheng M. R. Cell. 1996; Full Text Full Text PDF PubMed Scopus Google Scholar). a for these in a PDZ the PDZ domain in mouse to a that contains five of a Fanning A.S. C. J. A. Anderson J.M. PubMed Scopus Google Scholar). in the and may in PDZ domain as MAGI-1 mRNA to three that encode proteins with unique COOH The COOH of and and of unique and their by A protein that to was found primarily in the and of with a in the nucleus The COOH terminus of the splice and is The of and which additional via This region contains three of and that to the sequence for a bipartite nuclear localization This sequence consists of two followed by a of followed by a of in which three of the five are J. C. Cell. Full Text PDF PubMed Scopus Google Scholar). with the of nuclear localization signals in the COOH terminus of MAGI-1c, it was found primarily in the nucleus of cells of the sequence is or which the sequence for by S. Cell. Full Text PDF PubMed Scopus Google are in and the three nuclear localization a regulatory for nuclear localization of ZO-1, a MAGUK that was as a of the tight was found in the nucleus of cells (8Gottardi C.J. Arpin M. Fanning A.S. Louvard D. Proc. Natl. Acad. Sci. U. S. A. 1996; 93: 10779-10784Crossref PubMed Scopus (305) Google Scholar). ZO-1 in two proteins that are by the or of an the domain (1Anderson J.M. Balda M.S. Fanning A.S. Curr. Opin. Cell Biol. 1993; 5: 772-778Crossref PubMed Scopus (181) Google Scholar). The two and are in different cell types in a that with variants to localize to the nucleus of cultured cells (8Gottardi C.J. Arpin M. Fanning A.S. Louvard D. Proc. Natl. Acad. Sci. U. S. A. 1996; 93: 10779-10784Crossref PubMed Scopus (305) Google Scholar). In at two of the three MAGI-1 in cells and in mouse and was found in the nucleus cells used in this that is in the nucleus at a ZO-1 is from the nucleus. the subcellular distribution of is by in cell is In to mouse primarily This of in mouse with its nuclear that its is from that of The COOH-terminal unique to and that a the that the unique COOH of these two MAGI-1 proteins they are in and cell types they subcellular MAGI-1 is the known protein in which a GuK domain is with five PDZ domains and two WW domains and on sequence with similar domains from the PDZ and WW domains in MAGI-1 are predicted to with the MAGI-1 GuK domain as a for protein-protein as it in the proteins E. S. A. Rothschild A. A.M. Sheng M. J. Cell Biol. PubMed Scopus Google M. Y. A. M. Y. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google MAGI-1 the to with to different proteins the of ZO-1 and MAGI-1 in the nucleus is their suggests that they may participate in the of from the cell surface to the nucleus. to for the protein-protein interaction domains in MAGI-1, which to the of this of the MAGUK and for the of this and for and for the