SYT14L, especially its C2 domain, is involved in regulating melanocyte differentiation

Abstract Background The formation of dendrites by melanocytes is highly analogous to that process in neural cells. We previously reported that a C2 domain-containing protein, copine-1, is involved in the extension of dendrites by neural cells. However, the effect of C2 domain-containing proteins in...

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Bibliographic Details
Published in:Journal of dermatological science 2013-12, Vol.72 (3), p.246-251
Main Authors: Yoo, Jae Cheal, Lim, Tae yeon, Park, Jin Sung, Hah, Young-Sool, Park, Nammi, Hong, Seong-Geun, Park, Jae-Yong, Yoon, Tae-Jin
Format: Article
Language:English
Subjects:
Adenoviridae
Animals
C2 domain
Cell Differentiation
Cyclic AMP Response Element-Binding Protein - metabolism
Dendrite
Dendrites - physiology
Dermatology
Extracellular Signal-Regulated MAP Kinases - metabolism
HEK293 Cells
Humans
Melanocyte differentiation
Melanocytes - cytology
Melanocytes - physiology
Mice
Phosphorylation
Protein Structure, Tertiary
Synaptotagmins - physiology
SYT14L
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Summary:Abstract Background The formation of dendrites by melanocytes is highly analogous to that process in neural cells. We previously reported that a C2 domain-containing protein, copine-1, is involved in the extension of dendrites by neural cells. However, the effect of C2 domain-containing proteins in dendrite formation by melanocytes has not yet been elucidated. Objective The aim of this study was to screen novel C2 domain-containing proteins related to dendrite outgrowth in melanocytes and to investigate their precise roles in melanocyte dendrite formation during differentiation. Methods We transduced mouse melan-a melanocytes with a recombinant adenovirus expressing a C2 domain library. Dendrite elongation, melanin content, tyrosinase activity and Western blot analyses were conducted to elucidate the possible underlying mechanisms of action in melanocytes. Results Sixteen sets of C2 domain-containing proteins were identified whose over-expression resulted in dendrite lengthening. Among those, we focused on the C2 domain of SYT14L (truncated mutant of SYT14L) in this study. Forced expression of full length SYT14L or the C2 domain of SYT14L induced a significant elongation of dendrite length accompanied by the induction of melanocyte differentiation-related markers, including melanin synthesis, tyrosinase catalytic activity and the expression of tyrosinase (TYR), tyrosinase related protein-1 (TRP-1) and TRP-2. In addition, over-expression of either the C2 domain or the full length form of SYT14L significantly increased the phosphorylation of ERK and CREB. Conclusion These results suggest that SYT14L, especially its C2 domain, may play an important role in regulating melanocyte differentiation through the modulation of ERK and (or) CREB signaling.
ISSN:0923-1811
1873-569X
DOI:10.1016/j.jdermsci.2013.07.010