Ectopic expression of LIM‐nebulette (LASP2) reveals roles in cell migration and spreading

Deng, Xiaolong; Norris, Andrea; Panaviene, Zivile; Moncman, Carole L.

doi:10.1002/cm.20304

Cited by 23 publications

(28 citation statements)

References 19 publications

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“…Although LASP2 and LASP1 share high similarity in the structure [6], a few studies had discovered they had adverse distribution in some particular cellular position [9, 10]. Consistently, we detected an opposite distribution and function of LASP1 and LASP2 in CRC, which may be a part of the regulation networks in cancer progression.…”

Section: Discussionsupporting

confidence: 82%

LASP2 suppresses colorectal cancer progression through JNK/p38 MAPK pathway meditated epithelial-mesenchymal transition

et al. 2017

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BackgroundLASP2 (LIM and SH3 Protein 2) is a small focal adhesion protein belongs to nebulin protein family. As the newest member of nebulette family, the function of LASP2 remains to be identified.MethodsThe relationship between LASP2 expression and clinical characteristics of CRC was analyzed in 89 paraffin-embedded archived CRC specimens by immunohistochemistry (IHC). The effects of LASP2 on cell growth and migration were examined in vitro, using CCK-8 and transwell assays. Western blotting was performed to examine the impact of LASP2 on the SAPK/JNK and MAPK signaling pathways.ResultsIn the present study, we observed a decreased LASP2 expression in clinical colorectal cancer samples compared with paired normal tissues. A negative correlation was also found between LASP2 and poor prognosis of CRC patients. Gain- and loss-of-function approaches revealed that LASP2 plays inhibitory effects on the growth and migration of human CRC cells in vitro. Western-blot results showed that LASP2 could attenuate epithelial-mesenchymal transition (EMT) to accomplish its suppression on CRC aggression. In LASP2 knocked down CRC cells, EMT was inhibited along with the inactivation of JNK/p38 MAPK pathway. Consistently, treatment of JNK inhibitor (JNK inhibitor II) together with p38 inhibitor (SB203580) could resume the process of EMT. Interestingly, we found a negative relationship between LASP2 and LASP1 expression in both CRC cell lines and tumors tissues, which suggests their converse function in CRC progression.ConclusionsAll the findings indicated that LASP2 may play a significant role in suppressing CRC progression and provided a novel biomarker for CRC therapy.Electronic supplementary materialThe online version of this article (doi:10.1186/s12964-017-0179-9) contains supplementary material, which is available to authorized users.

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Section: Discussionsupporting

confidence: 82%

LASP2 suppresses colorectal cancer progression through JNK/p38 MAPK pathway meditated epithelial-mesenchymal transition

et al. 2017

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“…The strongest lasp-2 expression appears to be in brain; it is localized to actin filament bundles in lamellipodia of cultured neuroblastoma cells [37]. In vitro , lasp-2 crosslinks actin filaments [39] and its overexpression in fibroblasts increases cell spreading [40]. Lasp-2 also appears to be multifunctional since it localizes to different cytotskeletal structures in cardiomyocytes including the Z-disc, cell-cell contacts (intercalated discs) and focal adhesions (Figures 2 and 3) [39, 41].…”

Section: Functions Of the Nebulin Family: A Melting-potmentioning

confidence: 99%

“…Based on its numerous assembly patterns, lasp-2 probably has several cellular roles. It has been speculated that lasp-2 acts as a molecular scaffold that is important for actin filament and focal adhesion stabilization and organization [39, 40, 42, 43]. …”

Section: Functions Of the Nebulin Family: A Melting-potmentioning

confidence: 99%

The Nebulin family: an actin support group

Pappas¹,

Bliss²,

Zieseniß³

et al. 2011

Trends in Cell Biology

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Nebulin, a giant actin-binding protein, is the largest member of a family of proteins (including N-RAP, nebulette, lasp-1 and lasp-2) which are assembled in a variety of cytoskeletal structures and expressed in different tissues. For decades nebulin has been thought to act as a molecular ruler, specifying the precise length of actin filaments in skeletal muscle. However, emerging evidence suggests that nebulin should not be viewed as a ruler but as an actin filament stabilizer required for length maintenance. Nebulin has also recently been implicated in an array of regulatory functions independent of its role in actin filament length regulation. In this review, we discuss the current evolutionary, biochemical, and functional data for the nebulin family of proteins -a family whose members, both large and small, function as cytoskeletal scaffolds and stabilizers.

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“…A commercial monoclonal antibody raised against LASP1 also recognizes LIM-nebulette, nebulin and nebulette [22]. As LASP1 is not expressed in striated muscles [23], we used this antibody to probe 15% polyacrylamide gel replicas to examine the abundance of LIM-nebulette (Figure 8B).…”

Section: Resultsmentioning

confidence: 99%

Development transitions of thin filament proteins in rat extraocular muscles

Moncman

Andrade

McCool

et al. 2013

Experimental Cell Research

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Extraocular muscles are a unique subset of striated muscles. During postnatal development, the extraocular muscles undergo a number of myosin isoform transitions that occur between postnatal day 10 (P10) and P15. These include: 1) loss of embryonic myosin from the global layer resulting in the expression restricted to the orbital layer; 2) the onset of expression of extraocular myosin and the putative tonic myosin (myh 7b/14); and 3) the redistribution of nonmuscle myosin IIB from a subsarcolemma position to a sarcomeric distribution in the slow fibers of the global layer. For this study, we examined the postnatal appearance and distribution of α-actinin, tropomyosin, and nebulin isoforms during postnatal development of the rat extraocular muscles. Although sarcomeric α-actinin is detectable from birth, α-actinin 3 appears around P15. Both tropomyosin-1 and -2 are present from birth in the same distribution as in the adult animal. The expression of nebulin was monitored by gel electrophoresis and western blots. At P5–10, nebulin exhibits a lower molecular mass than observed P15 and later during postnatal development. The changes in α-actinin3 and nebulin expression between P10 and 15 coincide with transitions in myosin isoforms as detailed above. These data point to P10–P15 as the critical period for the maturation of the extraocular muscles, coinciding with eyelid opening.

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Ectopic expression of LIM‐nebulette (LASP2) reveals roles in cell migration and spreading

Cited by 23 publications

References 19 publications

LASP2 suppresses colorectal cancer progression through JNK/p38 MAPK pathway meditated epithelial-mesenchymal transition

LASP2 suppresses colorectal cancer progression through JNK/p38 MAPK pathway meditated epithelial-mesenchymal transition

The Nebulin family: an actin support group

Development transitions of thin filament proteins in rat extraocular muscles

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