Investigating lasp-2 in cell adhesion: new binding partners and roles in motility

Bliss, Katherine T.; Chu, Miensheng; Jones-Weinert, Colin M.; Gregorio, Carol C.

doi:10.1091/mbc.e12-10-0723

Cited by 23 publications

(31 citation statements)

References 46 publications

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“…LASP1 accumulates in focal adhesions, as well as in the leading edges of lamellipodia and tips of filopodia - the key structures for enabling cell adhesion, migration, and cellular communication [ 30 , 36 ]. This might be mediated by its SH3 domain as this domain enables LASP1 to bind to proline-rich domains of cytoskeleton proteins like zyxin, VASP and LPP - a common protein-protein interaction for proteins located close to the plasma membrane [ 7 ].…”

Section: Lasp1 Interaction With the Cytoskeletonmentioning

confidence: 99%

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An update on the LIM and SH3 domain protein 1 (LASP1): a versatile structural, signaling, and biomarker protein

Orth¹,

Cazes²,

Butt³

et al. 2014

Oncotarget

105

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The gene encoding the LIM and SH3 domain protein (LASP1) was cloned two decades ago from a cDNA library of breast cancer metastases. As the first protein of a class comprising one N-terminal LIM and one C-terminal SH3 domain, LASP1 founded a new LIM-protein subfamily of the nebulin group. Since its discovery LASP1 proved to be an extremely versatile protein because of its exceptional structure allowing interaction with various binding partners, its ubiquitous expression in normal tissues, albeit with distinct expression patterns, and its ability to transmit signals from the cytoplasm into the nucleus. As a result, LASP1 plays key roles in cell structure, physiological processes, and cell signaling. Furthermore, LASP1 overexpression contributes to cancer aggressiveness hinting to a potential value of LASP1 as a cancer biomarker.In this review we summarize published data on structure, regulation, function, and expression pattern of LASP1, with a focus on its role in human cancer and as a biomarker protein. In addition, we provide a comprehensive transcriptome analysis of published microarrays (n=2,780) that illustrates the expression profile of LASP1 in normal tissues and its overexpression in a broad range of human cancer entities.

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Section: Lasp1 Interaction With the Cytoskeletonmentioning

confidence: 99%

“…This interaction can be impaired by LASP1. Accordingly, the dynamic interplay of LASP1 and LASP2 at focal adhesions could mechanistically control cell adhesion by regulation of focal adhesion assembly [ 36 ].…”

Section: Lasp1 Interaction With the Cytoskeletonmentioning

confidence: 99%

An update on the LIM and SH3 domain protein 1 (LASP1): a versatile structural, signaling, and biomarker protein

Orth¹,

Cazes²,

Butt³

et al. 2014

Oncotarget

105

View full text Add to dashboard Cite

show abstract

“…Bicinchoninic acid assays and Ponceau S stains verified equivalent protein loading. Western blots were performed as described previously (Bliss et al, 2013) using rabbit anti-Tmod (1:1000), rabbit anti-Lmod3 (1:1000; Proteintech, Chicago, IL), monoclonal anti-GFP (1:3000; Covance, Dedham, MA), monoclonal anti-GAPDH (1:30,000; Sigma, St Louis, MO) and monoclonal antiMyc (1:1000, Upstate Biotechnology/Millipore, Billerica, MA; clone 9E10) antibodies.…”

Section: Western Blot Analysismentioning

confidence: 99%

Leiomodin 3 and Tropomodulin 4 have overlapping functions during skeletal myofibrillogenesis

Nworu

Kraft

Schnurr

et al. 2014

Journal of Cell Science

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Precise regulation of thin filament length is essential for optimal force generation during muscle contraction. The thin filament capping protein tropomodulin (Tmod) contributes to thin filament length uniformity by regulating elongation and depolymerization at thin filament ends. The leiomodins (Lmod1-3) are structurally related to Tmod1-4 and also localize to actin filament pointed ends, but in vitro biochemical studies indicate that Lmods act instead as robust nucleators. Here, we examined the roles of Tmod4 and Lmod3 during Xenopus skeletal myofibrillogenesis. Loss of Tmod4 or Lmod3 resulted in severe disruption of sarcomere assembly and impaired embryonic movement. Remarkably, when Tmod4-deficient embryos were supplemented with additional Lmod3, and Lmod3-deficient embryos were supplemented with additional Tmod4, sarcomere assembly was rescued and embryonic locomotion improved. These results demonstrate for the first time that appropriate levels of both Tmod4 and Lmod3 are required for embryonic myofibrillogenesis and, unexpectedly, both proteins can function redundantly during in vivo skeletal muscle thin filament assembly. Furthermore, these studies demonstrate the value of Xenopus for the analysis of contractile protein function during de novo myofibril assembly.

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“…NEBL encodes a nebulin-like protein. A shorter isoform of this protein (known as LASP2) is involved in cell-cell adhesion 13 , which has an important role in both the pathogenesis and progression of several tumor types 14 . Considering that cell-cell adhesion has been implicated in the tumorigenesis of pituitary adenoma 15 , we speculated that NEBL might be a compelling candidate gene for the association and have a role in pituitary adenoma tumorigenesis.…”

mentioning

confidence: 99%

Common variants at 10p12.31, 10q21.1 and 13q12.13 are associated with sporadic pituitary adenoma

Zhao

Wang

et al. 2015

Nat Genet

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Pituitary adenoma is one of the most common intracranial neoplasms, and its genetic basis remains largely unknown. To identify genetic susceptibility loci for sporadic pituitary adenoma, we performed a three-stage genome-wide association study (GWAS) in the Han Chinese population. We first analyzed genome-wide SNP data in 771 pituitary adenoma cases and 2,788 controls and then carried forward the promising variants for replication in another 2 independent sets (2,542 cases and 3,620 controls in total). We identified three new susceptibility loci below the genome-wide significance threshold (P < 5 × 10(-8)) in the combined analyses: 10p12.31 (rs2359536, P(meta) = 2.25 × 10(-10) and rs10828088, P(meta) = 6.27 × 10(-10)), 10q21.1 (rs10763170, P(meta) = 6.88 × 10(-10)) and 13q12.13 (rs17083838, P(meta) = 1.89 × 10(-8)). This study is the first GWAS to our knowledge on sporadic pituitary adenoma, and our results provide insight into the genetic basis of this disease.

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Investigating lasp-2 in cell adhesion: new binding partners and roles in motility

Cited by 23 publications

References 46 publications

An update on the LIM and SH3 domain protein 1 (LASP1): a versatile structural, signaling, and biomarker protein

An update on the LIM and SH3 domain protein 1 (LASP1): a versatile structural, signaling, and biomarker protein

Leiomodin 3 and Tropomodulin 4 have overlapping functions during skeletal myofibrillogenesis

Common variants at 10p12.31, 10q21.1 and 13q12.13 are associated with sporadic pituitary adenoma

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