Cell motility: proline-rich proteins promote protrusions

Holt, Mark R.; Koffer, Anna

doi:10.1016/s0962-8924(00)01876-6

Cited by 156 publications

(126 citation statements)

References 56 publications

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“…1 A). The PRMs in VopL closely resemble those found in the FH1 domains of formins, which are known to bind profilin and profilin-actin complexes (21).…”

Section: Vibrio Effector Vopl Contains Wh2 Domains and Proline-rich Rmentioning

confidence: 63%

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Arp2/3-independent assembly of actin by Vibrio type III effector VopL

Liverman¹,

Cheng

Trosky³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

144

178

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Microbial pathogens use a variety of mechanisms to disrupt the actin cytoskeleton during infection. Vibrio parahaemolyticus (V. para) is a Gram-negative bacterium that causes gastroenteritis, and new pandemic strains are emerging throughout the world. Analysis of the V. para genome revealed a type III secretion system effector, VopL, encoding three Wiskott-Aldrich homology 2 domains that are interspersed with three proline-rich motifs. Infection of HeLa cells with V. para induces the formation of long actin fibers in a VopL-dependent manner. Transfection of VopL promotes the assembly of actin stress fibers. In vitro, recombinant VopL potently induces assembly of actin filaments that grow at their barbed ends, independent of eukaryotic factors. Vibrio VopL is predicted to be a bacterial virulence factor that disrupts actin homeostasis during an enteric infection of the host.actin assembly ͉ microbial pathogenesis ͉ virulence ͉ stress fibers ͉ WH2 domains

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“…1 A). The PRMs in VopL closely resemble those found in the FH1 domains of formins, which are known to bind profilin and profilin-actin complexes (21).…”

Section: Vibrio Effector Vopl Contains Wh2 Domains and Proline-rich Rmentioning

confidence: 63%

“…Interspersed with the WH2 domains are three proline-rich motifs (PRMs). PRMs have many potential interacting partners, including WW domains, SH3 domains, and profilin (21) (Fig. 1 A).…”

Section: Vibrio Effector Vopl Contains Wh2 Domains and Proline-rich Rmentioning

confidence: 99%

Arp2/3-independent assembly of actin by Vibrio type III effector VopL

Liverman¹,

Cheng

Trosky³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

144

178

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show abstract

“…3A). It is known that some proline-rich sequences act as protein-protein interaction domains, which are implicated in various cellular processes such as cell motility and gene expression (30,31). Scapinin family proteins also contain proline-rich sequences that match or resemble those proline-rich motifs involved in protein-protein interactions (Fig.…”

Section: Fig 4 Expression Of Scapinin In Human Cell Lines and Tissuesmentioning

confidence: 99%

Scapinin, a Putative Protein Phosphatase-1 Regulatory Subunit Associated with the Nuclear Nonchromatin Structure

Sagara

Higuchi

Hattori

et al. 2003

Journal of Biological Chemistry

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It is thought that the nuclear nonchromatin structures, such as the nuclear matrix and lamina, play regulatory roles in gene expression. In this study, we identified an insoluble protein that was associated with the chromatin-depleted nuclear structure of proliferating human leukemia HL-60 cells. Preparation of the chromatin-depleted nuclear structure, referred to as the nuclear matrix-intermediate filament scaffold (Fey, E., Krochmalnic, G., and Penman, S. (1986) J. Cell. Biol. 102, 1654 -1665), involved cell extraction using a series of buffers containing Triton X-100, DNase I, and 2 M NaCl. A yeast two-hybrid assay revealed that this protein bound to the catalytic subunit of protein phosphatase-1 (PP1). Furthermore, it inhibited PP1 activity in vitro. We therefore named it scapinin (scaffold-associated PP1 inhibiting protein). cDNA cloning revealed that scapinin had two splicing variants of 448 amino acids (scapinin-S) and 518 amino acids (scapinin-L). Scapinin was down-regulated by differentiation in HL-60 cells. These results suggest that scapinin is a putative regulatory subunit of PP1 and is involved in transformed or immature phenotypes of HL-60 cells. We also describe the presence of scapinin family proteins from worm to human.Protein phosphatase-1 (PP1) 1 is a major eukaryotic serine/ threonine protein phosphatase regulating diverse cellular processes such as muscle contraction, glycogen metabolism, RNA processing, and neuronal signaling (1-3). The catalytic subunit of PP1 binds to regulatory subunits that are critical for substrate specificity and spatial control of PP1 within the cell (4).It is thought that the nuclear nonchromatin structures, such as the nuclear matrix (NM) and nuclear lamina, are implicated not only in the spatial segregation of chromatins but also in the regulation of various nuclear processes associated with them (5-7). However, the regulatory mechanisms of the nuclear nonchromatin structure are not fully understood. The ␣-catalytic subunit of PP1 is associated with NM during interphase, and PP1 is a mitotic lamin phosphatase (8, 9). Recruitment of PP1 to the nuclear envelope by a PP1-binding protein, protein kinase A-anchoring protein AKAP-149, is a prerequisite for nuclear lamina assembly at the end of mitosis (10). Identification of PP1-binding proteins associated with the nuclear nonchromatin structure will provide insights into the regulatory roles of PP1 in the nuclear structure and gene expression. Aberrant nuclear structures are hallmarks of neoplastic transformation (11). Nuclear lamins alter during differentiation and transformation (12, 13). Many reports have described striking alterations in the NM proteins induced by transformation (14 -18). The mechanisms and physiological importance of this phenomenon are not fully understood, and identification of the alterations may provide more insight into differentiation and transformation.HL-60 cells have been used as an in vitro model of differentiation because various compounds can cause differentiation of these cells into ...

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“…One class I motif (RPVPEPP, 528 -534) and three class II motifs (PPPPDR,(392)(393)(394)(395)(396)(397)(398)PTPPTK,(442)(443)(444)(445)(446)(447) were found in the MLN51 protein. In addition, we noticed the presence of a potential binding site for the profilin protein (LPPPPPP,(642)(643)(644)(645)(646)(647)(648)) that belongs to the PRM1 consensus site (Holt and Koffer, 2001) within the proline-rich part of the MLN51. Profilin requires a minimum of six to eight consecutive prolines for highaffinity binding and is believed to link signaling pathways to remodeling of the actin skeleton (Kay et al, 2000;Sohn and Goldshmidt-Clermont, 1994).…”

Section: Amino Acid Sequence Analysis Of Mln51 Proteinmentioning

confidence: 99%

Metastatic Lymph Node 51, a novel nucleo-cytoplasmic protein overexpressed in breast cancer

et al. 2002

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Metastatic Lymph Node 51 (MLN51) cDNA was isolated by differential screening of a human breast cancer metastasis cDNA library. MLN51 cDNA encodes a novel human protein of 703 residues that shares no significant homology to any known protein. However MLN51 is well conserved between vertebrate and invertebrate species suggesting an important biological function. The amino terminal half of the protein contains a coiled-coil domain and two potential nuclear localization signals (NLS). The carboxy terminal half contains one SH2 and four SH3 binding motifs. The coiled-coil domain promotes MLN51 oligomerization in transfected cells. When transiently expressed, the MLN51 protein is mainly found in the cytoplasm with a weak nuclear staining. However, deletion of the carboxy terminal half of the protein allows the targeting of the protein to the nucleus, demonstrating that the NLSs are functional. MLN51 is ubiquitously expressed in normal tissues. Human breast carcinomas show MLN51 overexpression in malignant epithelial cells. The uncommon association of protein -protein interaction domains often found either in nuclear or in cytoplasmic signaling proteins raises a possible nucleo-cytoplasmic function for MLN51.

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Cell motility: proline-rich proteins promote protrusions

Cited by 156 publications

References 56 publications

Arp2/3-independent assembly of actin by Vibrio type III effector VopL

Arp2/3-independent assembly of actin by Vibrio type III effector VopL

Scapinin, a Putative Protein Phosphatase-1 Regulatory Subunit Associated with the Nuclear Nonchromatin Structure

Metastatic Lymph Node 51, a novel nucleo-cytoplasmic protein overexpressed in breast cancer

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