The Wiskott-Aldrich syndrome is an inherited X-linked immunodeficiency characterized by thrombocytopenia, eczema, and a tendency toward lymphoid malignancy. Lymphocytes from affected individuals have cytoskeletal abnormalities, and monocytes show impaired motility. The Wiskott-Aldrich syndrome protein (WASP) is a multi-domain protein involved in cytoskeletal organization. In a two-hybrid screen, we identified the protein Cdc42-interacting protein 4 (CIP4) as a WASP interactor. CIP4, like WASP, is a Cdc42 effector protein involved in cytoskeletal organization. We found that the WASP-CIP4 interaction is mediated by the binding of the Src homology 3 domain of CIP4 to the proline-rich segment of WASP. Cdc42 was not required for this interaction. Co-expression of CIP4 and green fluorescent protein-WASP in COS-7 cells led to the association of WASP with microtubules. In vitro experiments showed that CIP4 binds to microtubules via its NH2 terminus. The region of CIP4 responsible for binding to active Cdc42 was localized to amino acids 383–417, and the mutation I398S abrogated binding. Deletion of the Cdc42-binding domain of CIP4 did not affect the colocalization of WASP with microtubules in vivo. We conclude that CIP4 can mediate the association of WASP with microtubules. This may facilitate transport of WASP to sites of substrate adhesion in hematopoietic cells. The Wiskott-Aldrich syndrome is an inherited X-linked immunodeficiency characterized by thrombocytopenia, eczema, and a tendency toward lymphoid malignancy. Lymphocytes from affected individuals have cytoskeletal abnormalities, and monocytes show impaired motility. The Wiskott-Aldrich syndrome protein (WASP) is a multi-domain protein involved in cytoskeletal organization. In a two-hybrid screen, we identified the protein Cdc42-interacting protein 4 (CIP4) as a WASP interactor. CIP4, like WASP, is a Cdc42 effector protein involved in cytoskeletal organization. We found that the WASP-CIP4 interaction is mediated by the binding of the Src homology 3 domain of CIP4 to the proline-rich segment of WASP. Cdc42 was not required for this interaction. Co-expression of CIP4 and green fluorescent protein-WASP in COS-7 cells led to the association of WASP with microtubules. In vitro experiments showed that CIP4 binds to microtubules via its NH2 terminus. The region of CIP4 responsible for binding to active Cdc42 was localized to amino acids 383–417, and the mutation I398S abrogated binding. Deletion of the Cdc42-binding domain of CIP4 did not affect the colocalization of WASP with microtubules in vivo. We conclude that CIP4 can mediate the association of WASP with microtubules. This may facilitate transport of WASP to sites of substrate adhesion in hematopoietic cells. Wiskott-Aldrich syndrome protein Cdc42-interacting protein 4 glutathione S-transferase polymerase chain reaction phosphate-buffered saline Src homology pleckstrin homology green fluorescent protein WASP-interacting protein 1,4-piperazinediethanesulfonic acid polyacrylamide gel electrophoresis tetramethylrhodamine B isothiocyanate GTPase binding domain Cdc42/Rac interacting and binding guanyl-5′-yl thiophosphate guanosine 5′-O-(thiotriphosphate) protein kinase C and casein kinase 2 substrate in neurons proline, serine, threonine phosphatase-interacting protein insulin-like growth factor 1-receptor β The Wiskott-Aldrich syndrome is an inherited X-linked immunodeficiency with associated thrombocytopenia, eczema, and a tendency toward development of malignancy of the lymphoreticular system (1.Aldrich R.A. Steinberg A.G. Campbell D.C. Pediatrics. 1954; 13: 133-138PubMed Google Scholar, 2.Rosen F.S. Cooper M.D. Wedgwood M.D. N. Engl. J. Med. 1995; 333: 431-440Crossref PubMed Scopus (342) Google Scholar). Affected individuals have lymphocytes that respond poorly to certain stimulants in vitro (3.Molina I.J. Sancho J. Terhorst C. Rosen F.S. Remold-O'Donnell E. J. Immunol. 1993; 151: 4383-4390PubMed Google Scholar, 4.Simon H.U. Mills G.B. Hashimoto S. Siminovitch K.A. J. Clin. Invest. 1992; 90: 1396-1405Crossref PubMed Scopus (75) Google Scholar) and show abnormalities of cytoskeletal structure (5.Gallego M.D. Santamaria M. Pena J. Molina I.J. Blood. 1997; 90: 3089-3097Crossref PubMed Google Scholar, 6.Kenney D. Cairns L. Remold-O'Donnel E. Peterson J. Rosen F.S. Parkman R. Blood. 1986; 68: 1329-1332Crossref PubMed Google Scholar, 7.Molina I.J. Kenney D.M. Rosen F.S. Remold-O'Donnell E. J. Exp. Med. 1992; 176: 867-874Crossref PubMed Scopus (118) Google Scholar, 8.Facchetti F. Blanzuoli L. Vermi W. Notarangelo L.D. Giliani S. Fiorini M. Fasth A. Stewart D.M. Nelson D.L. J. Pathol. 1998; 185: 99-107Crossref PubMed Scopus (50) Google Scholar). Impaired monocyte motility is also observed (9.Altman L.C. Snyderman R. Blaese R.M. J. Clin. Invest. 1974; 54: 486-493Crossref PubMed Scopus (63) Google Scholar, 10.Badolato R. Sozzani S. Malacarne F. Bresciani S. Fiorini M. Borsatti A. Albertini A. Mantovani A. Ugazio A.G. Notarangelo L.D. J. Immunol. 1998; 161: 1026-1033PubMed Google Scholar, 11.Zicha D. Allen W.E. Brickell P.M. Kinnon C. Dunn G.A. Jones G.E. Thrasher A.J. Br. J. Hematol. 1998; 101: 659-665Crossref PubMed Scopus (201) Google Scholar). The gene mutated in Wiskott-Aldrich syndrome was cloned in 1994, and was shown to encode a proline-rich protein of 502 amino acids (12.Derry J.M.J. Ochs H.D. Francke U. Cell. 1994; 78: 635-644Abstract Full Text PDF PubMed Scopus (816) Google Scholar, 13.Derry J.M.J. Ochs H.D. Francke U. Cell. 1994; 79: 923PubMed Google Scholar, 14.Kwan S. Hagemann T.L. Radtke B.E. Blaese R.M. Rosen F.S. Proc. Natl. Acad. Sci. U. S. A. 1995; 92: 4706-4710Crossref PubMed Scopus (96) Google Scholar). Although the function of WASP1 was not immediately apparent from knowledge of its primary structure, a variety of interactions have been discovered showing that WASP plays a role in cytoskeletal organization. The NH2 terminus of WASP binds to WASP-interacting protein (WIP), a protein with profilin binding and actin binding motifs, overexpression of which causes changes in cytoskeletal structure (15.Ramesh N. Anton I.M. Hartwig J.H. Geha R.S. Proc. Natl. Acad. Sci. U. S. A. 1997; 94: 14671-14676Crossref PubMed Scopus (302) Google Scholar). Missense mutations known to cause Wiskott-Aldrich syndrome impair the WASP-WIP interaction (16.Stewart D.M. Tian L. Nelson D.L. J. Immunol. 1999; 162: 5019-5024PubMed Google Scholar). A GBD/CRIB motif for binding the active forms of the small GTPases Rac and Cdc42, proteins that are involved in control of cytoskeletal organization, is present in WASP (18.Symons M. Derry J.M. Karlak B. Jiang S. Lemahieu V. McCormick F. Francke U. Abo A. Cell. 1996; 84: 723-734Abstract Full Text Full Text PDF PubMed Scopus (738) Google Scholar, 19.Kolluri R. Tolias K.F. Carpenter C.L. Rosen F.S. Kirchhausen T. Proc. Natl. Acad. Sci. U. S. A. 1996; 93: 5615-5618Crossref PubMed Scopus (187) Google Scholar, 20.Rivero-Lezcano O.M. Marcilla A. Sameshima J.H. Robbins K.C. Mol. Cell. Biol. 1995; 15: 5725-5731Crossref PubMed Scopus (279) Google Scholar). The proline-rich segment of WASP, between amino acids 310 and 420, interacts with a number of proteins containing SH3 domains, many of which are involved in the regulation of cytoskeletal structure. Among the SH3 proteins known to interact with WASP are the adaptor proteins Nck (21.Quilliam L.A. Lambert Q.T. Mickelson-Young L.A. Westwick J.K. Sparks A.B. Kay B.K. Jenkins N.A. Gilbert D.J. Copeland N.G. Der C.J. J. Biol. Chem. 1996; 271: 28772-28776Abstract Full Text Full Text PDF PubMed Scopus (132) Google Scholar, 22.She H.Y. Rockow S. Tang J. Nishimura R. Skolnik E.Y. Chen M. Margolis B. Li W. Mol. Biol. Cell. 1997; 8: 1709-1721Crossref PubMed Scopus (104) Google Scholar) and Grb2 (23.Zhu Q. Watanabe C. Liu T. Hollenbaugh D. Blaese R.M. Kanner S.B. Aruffo A. Ochs H.D. Blood. 1997; 90: 2680-2689Crossref PubMed Google Scholar,24.Banin S. Truong O. Katz D.R. Waterfield M.D. Brickell P.M. Gout I. Curr. Biol. 1996; 6: 981-988Abstract Full Text Full Text PDF PubMed Scopus (124) Google Scholar), Src family kinases (23.Zhu Q. Watanabe C. Liu T. Hollenbaugh D. Blaese R.M. Kanner S.B. Aruffo A. Ochs H.D. Blood. 1997; 90: 2680-2689Crossref PubMed Google Scholar, 25.Finan P.M. Soames C.J. Wilson L. Nelson D.L. Stewart D.M. Truong O. Hsuan J.J. Kellie S. J. Biol. Chem. 1996; 271: 26291-26295Abstract Full Text Full Text PDF PubMed Scopus (63) Google Scholar, 26.Cory G.O. MacCarthy-Morrogh L. Banin S. Gout I. Brickell P.M. Levinsky R.J. Kinnon C. Lovering R.C. J. Immunol. 1996; 157: 3791-3795PubMed Google Scholar, 27.Kinnon C. Cory G.O. MacCarthy-Morrogh L. Banin S. Gout I. Lovering R.C. Brickell P.M. Biochem. Soc. Trans. 1997; 25: 648-650Crossref PubMed Scopus (10) Google Scholar), phospholipase Cγ (23.Zhu Q. Watanabe C. Liu T. Hollenbaugh D. Blaese R.M. Kanner S.B. Aruffo A. Ochs H.D. Blood. 1997; 90: 2680-2689Crossref PubMed Google Scholar, 25.Finan P.M. Soames C.J. Wilson L. Nelson D.L. Stewart D.M. Truong O. Hsuan J.J. Kellie S. J. Biol. Chem. 1996; 271: 26291-26295Abstract Full Text Full Text PDF PubMed Scopus (63) Google Scholar), and Tec family kinases (26.Cory G.O. MacCarthy-Morrogh L. Banin S. Gout I. Brickell P.M. Levinsky R.J. Kinnon C. Lovering R.C. J. Immunol. 1996; 157: 3791-3795PubMed Google Scholar, 28.Miki H. Miura K. Takenawa T. EMBO J. 1996; 15: 5326-5335Crossref PubMed Scopus (544) Google Scholar). Motifs in the COOH terminus of WASP show homology to the actin-binding proteins verprolin (verprolin homology domain, amino acids 430–446) and cofilin (cofilin homology domain, amino acids 469–487) (18.Symons M. Derry J.M. Karlak B. Jiang S. Lemahieu V. McCormick F. Francke U. Abo A. Cell. 1996; 84: 723-734Abstract Full Text Full Text PDF PubMed Scopus (738) Google Scholar, 29.Miki H. Tanekawa T. Biochem. Biophys. Res. Commun. 1998; 243: 73-78Crossref PubMed Scopus (113) Google Scholar). WASP has been shown to interact directly with actin through the verprolin homology domain (30.Machesky L.M Insall R.H. Curr. Biol. 1998; 8: 1347-1356Abstract Full Text Full Text PDF PubMed Scopus (728) Google Scholar). A WASP homolog expressed in neural and other tissues, N-WASP, has the ability to depolymerize actin filaments in vitro (28.Miki H. Miura K. Takenawa T. EMBO J. 1996; 15: 5326-5335Crossref PubMed Scopus (544) Google Scholar, 29.Miki H. Tanekawa T. Biochem. Biophys. Res. Commun. 1998; 243: 73-78Crossref PubMed Scopus (113) Google Scholar). WASP, N-WASP, and the related proteins Scar1 in human and Bee1/Las17 in interact with the a of actin D. T. Li R. Curr. Biol. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar, D. W. Abo A M.D. Curr. Biol. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar). the of the Curr. Biol. 1997; Full Text Full Text PDF PubMed Scopus Google Scholar). that WASP is a of Cdc42/Rac and has the actin via actin-binding and of the SH3 protein interactions may a role in of WASP of to and through WASP. We a two-hybrid to for WASP-interacting WASP-interacting a of the protein This protein was identified as interacting with the active of Cdc42 J. E. H. R. Cell. 1993; Full Text PDF PubMed Scopus Google Scholar). CIP4 is a acid that has an domain of function with homology to the NH2 of the kinase and the which was the The region of the protein acids was shown to interact with Cdc42, not a GBD/CRIB SH3 domain is found in the COOH terminus of We a of the of and the of of CIP4 WASP and actin cytoskeletal structure in COS-7 cells. We the two-hybrid J. R. R. K. in and Scholar). and from of human for this system was from The was as (16.Stewart D.M. Tian L. Nelson D.L. J. Immunol. 1999; 162: 5019-5024PubMed Google Scholar, D. S. F. Notarangelo L.D. Nelson D.L. J. Clin. Invest. 1996; PubMed Scopus Google Scholar) WASP as in the from with the The of interaction of the interaction was with a containing an of protein that was with the from R. and with a containing an of human domain that was a from A WASP was cloned in to and for in vitro by for A CIP4 from a from of was cloned This CIP4 was as a to CIP4 and CIP4 for in vitro and for of CIP4 was cloned a of the that was to an in to CIP4 in cells. mutations by with containing the the of CIP4 and WASP by the with the sites of the was for of the to the of the In vitro binding of WASP with CIP4, and WASP CIP4 with Cdc42 the In an in protein was with a binding in the of an protein to of protein to was 4 for 2 with of the in protein in in the of Cdc42, with in a of with the to the protein and from the and interaction by in gel containing This protein was an gel and the gel to protein that to the protein as a the WASP CIP4 was by in the system in the of proteins expressed the from in of of and by was to a of and the was for The was for with and binding of the was and 4 The and of the proteins was by by proteins with the immediately by of the protein to in and 2 for and with was as A CIP4 was cloned and expressed in E. The was by to with of by for and and by as was from the by to and from and from was from and was from was as D. J. Biol. 1993; PubMed Scopus Google Scholar). was the COS-7 cells in with and 2 by COS-7 cells with and in with 4 for and for The was with with and was to a of 4 for 2 protein of a in was and the 4 for The was with and proteins by by by in with for by as by the The binding experiments as S. Nelson D. M. M. Proc. Natl. Acad. Sci. U. S. A. 1999; PubMed Scopus Google Scholar). of in vitro CIP4 CIP4 was in of containing The was for 4 in a of was with of microtubules for in the of The and CIP4 of in and for in a the and for the of CIP4 and its by by The with to that an of microtubules was the gel in COS-7 cells with in the of by in cells and by human and for as J. R. Scholar). cells and by for H. T. Takenawa T. 1998; PubMed Scopus Google Scholar) by in for by was an with and of through the cells WASP-interacting identified in the two-hybrid number a of the protein CIP4, a amino acid protein that been identified as an containing protein with homology to the kinase that interacts with the active of Cdc42 Curr. Biol. 1997; Full Text Full Text PDF PubMed Scopus Google Scholar). The acid of was to of the CIP4 number with the of a C in the The CIP4 amino acids The interaction was to the interaction of CIP4 with protein the domain of was in the two-hybrid system not The region of WASP responsible for interaction with CIP4 was by mutation in the two-hybrid This showed that CIP4 with a WASP amino acids to interact with a WASP amino acids not the WASP has the and the proline-rich region of interaction the CIP4 SH3 domain directly to WASP in the proline-rich the homolog of Cdc42 is to the human the binding of Cdc42 to WASP and CIP4 to the interaction. We an in vitro binding to the of interaction. The interaction between in vitro WASP of and and is shown in CIP4 to WASP amino acids and which the region and the WASP the region and CIP4 not the WASP was present This that the proline-rich region of WASP is for CIP4 binding. WASP to which the CIP4 SH3 WASP which the region the actin binding SH3 This may to a WASP interaction between and of the which may the proline-rich region for binding to the CIP4 SH3 domain M. H. K. S. T. C. Takenawa T. J. Biol. Chem. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar, I. S. Kay R. R.A. J. Biol. Chem. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar). WASP the region and to the CIP4 SH3 A CIP4 the SH3 domain WASP that the WASP-CIP4 interaction is mediated by the binding of the CIP4 SH3 domain to the region of WASP, and that the of the WASP has this binding. that the interaction can of Cdc42 the binding of in WASP to CIP4 and the active Cdc42 was shown in a of WASP the the ability to CIP4, Cdc42 binding is This that CIP4 can to WASP in the of Cdc42 binding. the COS-7 cells with and with CIP4 as shown in The CIP4 did not show binding to WASP, showing the of the CIP4 SH3 expressed the CIP4 SH3 domain localized in the as by not and was not for interaction with WASP by The primary of CIP4 not the GBD/CRIB motif of the binding of We a of CIP4 for the ability to interact with the active of in CIP4 with with the active not to the forms The Cdc42 to CIP4 of shown in CIP4 CIP4 amino acids and with Cdc42, CIP4 did A of mutations in this region of the CIP4 that the mutation I398S abrogated binding of CIP4 to active Cdc42 4 We conclude that the CIP4 amino acids and the amino acid are for Cdc42 binding to Wiskott-Aldrich syndrome show abnormalities of and and of (3.Molina I.J. Sancho J. Terhorst C. Rosen F.S. Remold-O'Donnell E. J. Immunol. 1993; 151: 4383-4390PubMed Google Scholar, 4.Simon H.U. Mills G.B. Hashimoto S. Siminovitch K.A. J. Clin. Invest. 1992; 90: 1396-1405Crossref PubMed Scopus (75) Google Scholar, M.D. Santamaria M. Pena J. Molina I.J. Blood. 1997; 90: 3089-3097Crossref PubMed Google Scholar, 6.Kenney D. Cairns L. Remold-O'Donnel E. Peterson J. Rosen F.S. Parkman R. Blood. 1986; 68: 1329-1332Crossref PubMed Google Scholar, 7.Molina I.J. Kenney D.M. Rosen F.S. Remold-O'Donnell E. J. Exp. Med. 1992; 176: 867-874Crossref PubMed Scopus (118) Google Scholar, 8.Facchetti F. Blanzuoli L. Vermi W. Notarangelo L.D. Giliani S. Fiorini M. Fasth A. Stewart D.M. Nelson D.L. J. Pathol. 1998; 185: 99-107Crossref PubMed Scopus (50) Google Scholar, L.C. Snyderman R. Blaese R.M. J. Clin. Invest. 1974; 54: 486-493Crossref PubMed Scopus (63) Google Scholar, 10.Badolato R. Sozzani S. Malacarne F. Bresciani S. Fiorini M. Borsatti A. Albertini A. Mantovani A. Ugazio A.G. Notarangelo L.D. J. Immunol. 1998; 161: 1026-1033PubMed Google Scholar, 11.Zicha D. Allen W.E. Brickell P.M. Kinnon C. Dunn G.A. Jones G.E. Thrasher A.J. Br. J. Hematol. 1998; 101: 659-665Crossref PubMed Scopus (201) Google Scholar). a role for WASP in actin overexpression of WASP the of (18.Symons M. Derry J.M. Karlak B. Jiang S. Lemahieu V. McCormick F. Francke U. Abo A. Cell. 1996; 84: 723-734Abstract Full Text Full Text PDF PubMed Scopus (738) Google Scholar). In to the role of CIP4 WASP with the COOH terminus was COS-7 cells in the of In the of CIP4, the colocalization of with was observed in cells with by (18.Symons M. Derry J.M. Karlak B. Jiang S. Lemahieu V. McCormick F. Francke U. Abo A. Cell. 1996; 84: 723-734Abstract Full Text Full Text PDF PubMed Scopus (738) Google Scholar), of cells of in the by the of The protein in with In cells with a in was observed with a and not This has been by Curr. Biol. 1997; Full Text Full Text PDF PubMed Scopus Google Scholar). was with of and in cells did not with and a to that in cells with of the cells showed a of and the other showed in of a This was not observed in cells with We the between the and microtubules by the cells with with CIP4, cells a with microtubules from a to the of structure was in cells and was between and microtubules In cells and CIP4, a of is that with in cells in of of microtubules. for CIP4 in cells with WASP a of CIP4 with of CIP4 to microtubules was not observed in cells of CIP4 WASP with microtubules. COS-7 cells with in the of cells and WASP was by and was by by and The and for of colocalization and We the ability of CIP4 and CIP4 to to microtubules by an in vitro vitro CIP4 CIP4 with microtubules. by of CIP4 amino acids and as as CIP4, with microtubules as shown in CIP4 and CIP4 did not with microtubules that the of CIP4 binding. CIP4 and CIP4 from the by microtubules CIP4, that the of CIP4 binds to microtubules experiments showed that CIP4 and the binding for also to microtubules not CIP4 showed a of the the in vitro and the in of CIP4 WASP that CIP4 with microtubules. We the of CIP4 in COS-7 cells and in primary human a COS-7 and a human in with and is association of CIP4 with microtubules in We conclude that CIP4 with microtubules in and that the in the cells CIP4 is the of the of protein has been that the and WASP in cells by the actin (18.Symons M. Derry J.M. Karlak B. Jiang S. Lemahieu V. McCormick F. Francke U. Abo A. Cell. 1996; 84: 723-734Abstract Full Text Full Text PDF PubMed Scopus (738) Google Scholar). A of in cells CIP4 has also been observed by not and Curr. Biol. 1997; Full Text Full Text PDF PubMed Scopus Google Scholar). is that in the of CIP4, actin is actin is This may WASP in an to to microtubules. The domain of family has been to with S. J. Biol. Chem. 1998; Full Text Full Text PDF PubMed Scopus Google Scholar). have that WASP has a domain in its amino acids (28.Miki H. Miura K. Takenawa T. EMBO J. 1996; 15: 5326-5335Crossref PubMed Scopus (544) Google Scholar), we the association of WASP in the of CIP4 was mediated by binding of WASP to microtubules through its domain, through the binding of CIP4 expressed with in COS-7 cells CIP4 been for WASP and binding by in vitro in the of CIP4, which has the ability to to WASP and WASP to the of microtubules The CIP4 which the binding binds to WASP in a expressed in COS-7 cells CIP4 showed the in as the protein not with CIP4 the as CIP4 in the that are of WASP with did not the of microtubules. This that CIP4 binding is required for WASP to with microtubules. CIP4 which the SH3 domain, to microtubules not to WASP in not This was to cause WASP to a is an of CIP4 amino acids We have shown by in vitro binding that CIP4 amino acids between for binding active Cdc42 and WASP binding vitro not and WASP to the of microtubules that the and of CIP4 are required to cause the association of WASP with microtubules in cells. Cdc42 binding by CIP4 did not to for of WASP to microtubules. CIP4 was identified in a two-hybrid as a protein interacting with active Cdc42 and was found to have homology in the region to the kinase and to the related kinase Curr. Biol. 1997; Full Text Full Text PDF PubMed Scopus Google Scholar). This region of homology was the The domain is found in the NH2 terminus of a variety of proteins from to M. R. H. S. M. M. M. D. J. Biochem. 1998; PubMed Scopus Google Scholar, A. Cell. 1995; Full Text PDF PubMed Scopus Google Scholar). 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Chem. 1998; Full Text Full Text PDF PubMed Scopus Google Scholar). experiments are to Cdc42 has CIP4 adaptor function in that other domain proteins microtubules and as to The proteins kinase C and casein kinase 2 substrate in and serine, threonine phosphatase-interacting are to CIP4 in that have an domain and a SH3 domain M. R. H. S. M. M. M. D. J. Biochem. 1998; PubMed Scopus Google Scholar, L.A. J. Biol. Chem. 1998; Full Text Full Text PDF PubMed Scopus Google Scholar). was shown to WASP via its SH3 domain, in of WASP from to a D. L.A. J. Biol. Chem. 1998; Full Text Full Text PDF PubMed Scopus Google Scholar). The related protein which is to that the SH3 domain, was found to with in a B. J. Mol. Biol. Cell. 1999; PubMed Scopus Google Scholar). which is the homolog of the human binds the protein via its SH3 domain B. J. M. M. 1999; PubMed Scopus Google Scholar). which is to in a that the and actin E. Curr. 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The from the as the also to the substrate by In the the to the of and the microtubules are the in M. I. 1997; PubMed Scopus Google Scholar). This that the microtubules may to the sites In the structure is the In the microtubules to the and of the I. O. J. Biol. 1999; PubMed Scopus Google Scholar, K. J. Biol. 1998; PubMed Scopus Google Scholar). may that CIP4 is a of a WASP and other proteins the microtubules for to sites of structure experiments the of CIP4 in cells of this In we have shown that the Cdc42 effector CIP4 and WASP and that CIP4 the association of WASP with microtubules. This the of the as a which plays a role in of and We for and for and with the
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