TY  - JOUR
A1  - Orth, Martin F.
A1  - Cazes, Alex
A1  - Butt, Elke
A1  - Grunewald, Thomas G. P.
T1  - An update on the LIM and SH3 domain protein 1 (LASP1): a versatile structural, signaling, and biomarker protein
JF  - Oncotarget
N2  - 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.
KW  - LASP1
KW  - cancer
KW  - biomarker
KW  - microRNA
KW  - nucleo-cytoplasmic
Y1  - 2015
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-144546
VL  - 6
IS  - 1
ER  - 
TY  - JOUR
A1  - Vaman V. S., Anjana
A1  - Poppe, Heiko
A1  - Houben, Roland
A1  - Grunewald, Thomas G. P.
A1  - Goebeler, Matthias
A1  - Butt, Elke
T1  - LASP1, a Newly Identified Melanocytic Protein with a Possible Role in Melanin Release, but Not in Melanoma Progression
JF  - PLoS One
N2  - The LIM and SH3 protein 1 (LASP1) is a focal adhesion protein. Its expression is increased in many malignant tumors. However, little is known about the physiological role of the protein. In the present study, we investigated the expression and function of LASP1 in normal skin, melanocytic nevi and malignant melanoma. In normal skin, a distinct LASP1 expression is visible only in the basal epidermal layer while in nevi LASP1 protein is detected in all melanocytes. Melanoma exhibit no increase in LASP1 mRNA compared to normal skin. In melanocytes, the protein is bound to dynamin and mainly localized at late melanosomes along the edges and at the tips of the cell. Knockdown of LASP1 results in increased melanin concentration in the cells. Collectively, we identified LASP1 as a hitherto unknown protein in melanocytes and as novel partner of dynamin in the physiological process of membrane constriction and melanosome vesicle release.
KW  - cell membranes
KW  - vesicles
KW  - melanoma cells
KW  - melanomas
KW  - melanocytes
KW  - membrane proteins
KW  - melanin
KW  - cell staining
Y1  - 2015
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-125994
VL  - 10
IS  - 6
ER  -