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J. Biol. Chem., Vol. 278, Issue 20, 17945-17952, May 16, 2003

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The Nucleo-cytoplasmic Actin-binding Protein CapG Lacks a Nuclear Export Sequence Present in Structurally Related Proteins^*

Katrien Van Impe^§, Veerle De Corte^¶, Ludwig Eichinger, Erik Bruyneel^**, Marc Mareel^**, Joël Vandekerckhove, and Jan Gettemans^¶

From the  Department of Biochemistry, Flanders Interuniversity Institute for Biotechnology, Faculty of Medicine and Health Sciences, Ghent University, Rommelaere Institute, Albert Baertsoenkaai 3, B-9000 Ghent, Belgium and Flanders Interuniversity Institute for Biotechnology, the  Institut für Biochemie I, Medizinische Fakultät, Universität zu Köln, Joseph-Stelzmann-Strasse 52, 50931 Köln, Germany, and the ^** Laboratory of Experimental Cancerology, Department of Radiotherapy and Nuclear Medicine, Ghent University Hospital, De Pintelaan 185, B-9000 Ghent, Belgium

Despite thorough structure-function analyses, it remains unclear how CapG, a ubiquitous F-actin barbed end capping protein that controls actin microfilament turnover in cells, is able to reside in the nucleus and cytoplasm, whereas structurally related actin-binding proteins are predominantly cytoplasmic. Here we report the molecular basis for the different subcellular localization of CapG, severin, and fragminP. Green fluorescent protein-tagged fragminP and severin accumulate in the nucleus upon treatment of transfected cells with the CRM1 inhibitor leptomycin B. We identified a nuclear export sequence in severin and fragminP, which is absent in CapG. Deletion of amino acids Met¹-Leu²⁷ resulted in nuclear accumulation of severin and fragminP. Tagging this sequence to CapG triggered nuclear export, whereas mutation of single leucine residues (Leu¹⁷, Leu²¹, and Leu²⁷) in the export sequence inhibited nuclear export. Based on these findings, a nuclear export signal was identified in myopodin, a muscle-specific actin-binding protein, and the Bloom syndrome protein, a RecQ-like helicase. Deletion of the myopodin nuclear export sequence blocked invasion into collagen type I of C2C12 cells transiently overexpressing myopodin. Our findings explain regulated subcellular targeting of distinct classes of actin-binding proteins.

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