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(Circulation Research. 2006;98:306.)
© 2006 American Heart Association, Inc.

Editorials

Organizing Motility

LIM Domains, LPP, and Smooth Muscle Migration

Mark W. Majesky

From the Carolina Cardiovascular Biology Center, and Departments of Medicine & Genetics, University of North Carolina at Chapel Hill.

Correspondence to Mark W. Majesky, PhD, Carolina Cardiovascular Biology Center, 8200 MBRB, Campus Box 7126, University of North Carolina, Chapel Hill, NC 27599-7126. E-mail mmajesky@med.unc.edu

See related article, pages 378–385

Key Words: smooth muscle cells • LIM domain • migration • focal adhesions

An extract of the first 250 words of the full text is provided, because this article has no abstract.

	Introduction

 
Vascular smooth muscle cells (SMCs) acquire a highly specialized cytoskeleton during development that is organized for efficient transmission of contractile force. This SMC cytoskeleton must be extensively reorganized to support directed cell migrations that are required for repair of arterial injury. Particularly important in this reorganization process are adaptor proteins that mediate the assembly of multiprotein complexes involved in cell adhesion, lamellipodial extensions, signal transduction, and transcriptional activation. One such adaptor protein is called lipoma-preferred partner (LPP), a member of the LIM domain–containing protein family, most closely related to zxyin, ajuba, LIM domain–containing protein-1 (LIMD1), and thyroid receptor-interacting protein-6 (TRIP6).¹ Evidence to suggest that LPP is a smooth muscle–restricted LIM protein that plays an important role in SMC migration after arterial injury is reported by Gorenne et al in this issue of Circulation Research.²

	Discovery of LPP as a Translocation Partner in Human Lipomas

 
LPP was discovered as a component of t(3:12) chromosome translocations found in benign tumors of human adipose tissue (lipomas).³ The chromosome 3 breakpoint occurred in a 400-kb genomic locus that encoded a protein with proline-rich sequences and leucine zipper motifs at its N terminus and three LIM domains at its C terminus. The t(3:12) translocation produced a fusion protein containing the N-terminal DNA binding domain of HMGIC fused to the C-terminal LIM domains of a protein encoded by the chromosome 3 locus. The latter was given the name LIM domain–containing lipoma-preferred partner (LPP).³ The lipoma-associated fusion protein is localized to the nucleus⁴ and can function as a transcription activator.⁵ Translocations involving the LIM domains of . . . [Full Text of this Article]

Related Article:

LPP Expression During In Vitro Smooth Muscle Differentiation and Stent-Induced Vascular Injury

I. Gorenne, L. Jin, T. Yoshida, J.M. Sanders, I.J. Sarembock, G.K. Owens, A.P. Somlyo, and A.V. Somlyo
Circ. Res. 2006 98: 378-385. [Abstract] [Full Text] [PDF]

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