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

Jae Cheal Yoo, Tae yeon Lim, Jin Sung Park, Young Sool Hah, Nammi Park, Seong Geun Hong, Jae-Yong Park, Tae Jin Yoon

Research output: Contribution to journalArticle

4 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)246-251
Number of pages6
JournalJournal of Dermatological Science
Volume72
Issue number3
DOIs
Publication statusPublished - 2013 Dec 1
Externally publishedYes

Fingerprint

Melanocytes
Dendrites
Monophenol Monooxygenase
Melanins
Elongation
Proteins
Phosphorylation
Catalyst activity
Modulation
C2 Domains
Differentiation Antigens
Adenoviridae
Western Blotting

Keywords

  • C2 domain
  • Dendrite
  • Melanocyte differentiation
  • SYT14L

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Dermatology

Cite this

Yoo, J. C., Lim, T. Y., Park, J. S., Hah, Y. S., Park, N., Hong, S. G., ... Yoon, T. J. (2013). SYT14L, especially its C2 domain, is involved in regulating melanocyte differentiation. Journal of Dermatological Science, 72(3), 246-251. https://doi.org/10.1016/j.jdermsci.2013.07.010

SYT14L, especially its C2 domain, is involved in regulating melanocyte differentiation. / Yoo, Jae Cheal; Lim, Tae yeon; Park, Jin Sung; Hah, Young Sool; Park, Nammi; Hong, Seong Geun; Park, Jae-Yong; Yoon, Tae Jin.

In: Journal of Dermatological Science, Vol. 72, No. 3, 01.12.2013, p. 246-251.

Research output: Contribution to journalArticle

Yoo, Jae Cheal ; Lim, Tae yeon ; Park, Jin Sung ; Hah, Young Sool ; Park, Nammi ; Hong, Seong Geun ; Park, Jae-Yong ; Yoon, Tae Jin. / SYT14L, especially its C2 domain, is involved in regulating melanocyte differentiation. In: Journal of Dermatological Science. 2013 ; Vol. 72, No. 3. pp. 246-251.
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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.",
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AU - Lim, Tae yeon

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AU - Hong, Seong Geun

AU - Park, Jae-Yong

AU - Yoon, Tae Jin

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