A novel transcript encoding truncated LIM kinase 2 is specifically expressed in male germ cells undergoing meiosis
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Authors: Takahashi, H; Koshimizu, U; Nakamura, T
Abstract
LIM kinases, composed of LIMK1 and LIMK2, have unique structural features that contain two LIM motifs at the N-terminus and a catalytic domain at the C-terminus. We report evidence of a novel type of mouse LIMK2 (Limk2) transcript specifically expressed in testis. cDNA cloning showed this Limk2 variant, designated tLimk2, lacked LIM domains at the N-terminus, due to usage of a testis-specific, alternative initiation exon. In Northern blot analysis, tLimk2 was detected in intact adult testis, but not in germ-cell-deficient or immature testis, indicating the stage-specific expression of tLimk2 in spermatogenic cells. In situ hybridization clearly demonstrated that tLimk2 was restrictedly expressed in differentiated germ cells (pachytene spermatocytes to round spermatids) and not expressed in early stages of spermatogenic cells and somatic cells in testis. These results suggested the possibility that the tLimk2 product is involved in spermatogenesis, especially in meiotic and/or postmeiotic processes. (C) 1998 Academic Press.
Different activity regulation and subcellular localization of LIMK1 and LIMK2 during cell cycle transition
EXPERIMENTAL CELL RESEARCH
Authors: Sumi, T; Hashigasako, A; Matsumoto, K; Nakamura, T
Abstract
LIM kinases (LIMK1 and LIMK2) regulate actin cytoskeletal reorganization through phosphorylating and inactivating cofilin, an actin-depolymerizing factor of actin filaments. Here, we describe a detailed analysis of the cell-cycle-dependentactivity of LIMK2, and a subcellular localization of LIMK1 and LIMK2. The activity of LIMK2, distinct from LIMK1, toward cofilin phosphorylation did not change in the normal cell division cycle. In contrast, LIMK2 was hyperphosphorylated and its activity was markedly increased when HeLa cells were synchronized at mitosis with nocodazole treatment. Immunofluorescence analysis showed that LIMK1 was localized at cell-cell adhesion sites in interphase and prophase, redistributed to the spindle poles during prometaphase to anaphase, and accumulated at the cleavage furrow in telophase. In contrast, LIMK2 was diffusely localized in the cytoplasm during interphase, redistributed to the mitotic spindle, and finally to the spindle midzone during anaphase to telophase. These findings suggest that LIMK2 is activated in response to microtubule disruption, and that LIMK1 and LIMK2 may play different roles in regulating for the mitotic spindle organization, chromosome segregation, and cytokinesis during the cell division cycle. (c) 2005 Elsevier Inc. All rights reserved.